data_7HD0
# 
_entry.id   7HD0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HD0         pdb_00007hd0 10.2210/pdb7hd0/pdb 
WWPDB D_1001407318 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HD0 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                        18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                            114.023   1   ? ? ? ? 
3 non-polymer syn '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-5-yl)propan-1-ol' 275.330   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                    35.453    1   ? ? ? ? 
5 water       nat water                                                                             18.015    426 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                            TFA   
3 '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-5-yl)propan-1-ol' A1A6Y 
4 'CHLORIDE ION'                                                                    CL    
5 water                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A6Y non-polymer         . '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-5-yl)propan-1-ol' ? 'C12 H13 N5 O S' 
275.330 
ALA   'L-peptide linking' y ALANINE                                                                           ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                          ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                        ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                   ? 'C4 H7 N O4'     
133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                    ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                          ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                         ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                   ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                           ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                         ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                             ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                           ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                            ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                        ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                     ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                           ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                            ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                            ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                         ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                          ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                            ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A6Y 1   202 201  A1A6Y LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 105  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 1289 HOH   HOH A . 
F 5 HOH   4   304 153  HOH   HOH A . 
F 5 HOH   5   305 493  HOH   HOH A . 
F 5 HOH   6   306 625  HOH   HOH A . 
F 5 HOH   7   307 15   HOH   HOH A . 
F 5 HOH   8   308 196  HOH   HOH A . 
F 5 HOH   9   309 229  HOH   HOH A . 
F 5 HOH   10  310 661  HOH   HOH A . 
F 5 HOH   11  311 209  HOH   HOH A . 
F 5 HOH   12  312 11   HOH   HOH A . 
F 5 HOH   13  313 109  HOH   HOH A . 
F 5 HOH   14  314 1301 HOH   HOH A . 
F 5 HOH   15  315 136  HOH   HOH A . 
F 5 HOH   16  316 281  HOH   HOH A . 
F 5 HOH   17  317 192  HOH   HOH A . 
F 5 HOH   18  318 76   HOH   HOH A . 
F 5 HOH   19  319 124  HOH   HOH A . 
F 5 HOH   20  320 278  HOH   HOH A . 
F 5 HOH   21  321 39   HOH   HOH A . 
F 5 HOH   22  322 9    HOH   HOH A . 
F 5 HOH   23  323 1290 HOH   HOH A . 
F 5 HOH   24  324 17   HOH   HOH A . 
F 5 HOH   25  325 393  HOH   HOH A . 
F 5 HOH   26  326 151  HOH   HOH A . 
F 5 HOH   27  327 86   HOH   HOH A . 
F 5 HOH   28  328 15   HOH   HOH A . 
F 5 HOH   29  329 1283 HOH   HOH A . 
F 5 HOH   30  330 1295 HOH   HOH A . 
F 5 HOH   31  331 225  HOH   HOH A . 
F 5 HOH   32  332 18   HOH   HOH A . 
F 5 HOH   33  333 236  HOH   HOH A . 
F 5 HOH   34  334 469  HOH   HOH A . 
F 5 HOH   35  335 964  HOH   HOH A . 
F 5 HOH   36  336 409  HOH   HOH A . 
F 5 HOH   37  337 2    HOH   HOH A . 
F 5 HOH   38  338 164  HOH   HOH A . 
F 5 HOH   39  339 21   HOH   HOH A . 
F 5 HOH   40  340 247  HOH   HOH A . 
F 5 HOH   41  341 155  HOH   HOH A . 
F 5 HOH   42  342 18   HOH   HOH A . 
F 5 HOH   43  343 140  HOH   HOH A . 
F 5 HOH   44  344 165  HOH   HOH A . 
F 5 HOH   45  345 241  HOH   HOH A . 
F 5 HOH   46  346 8    HOH   HOH A . 
F 5 HOH   47  347 1300 HOH   HOH A . 
F 5 HOH   48  348 630  HOH   HOH A . 
F 5 HOH   49  349 320  HOH   HOH A . 
F 5 HOH   50  350 57   HOH   HOH A . 
F 5 HOH   51  351 337  HOH   HOH A . 
F 5 HOH   52  352 92   HOH   HOH A . 
F 5 HOH   53  353 93   HOH   HOH A . 
F 5 HOH   54  354 42   HOH   HOH A . 
F 5 HOH   55  355 354  HOH   HOH A . 
F 5 HOH   56  356 5    HOH   HOH A . 
F 5 HOH   57  357 296  HOH   HOH A . 
F 5 HOH   58  358 33   HOH   HOH A . 
F 5 HOH   59  359 70   HOH   HOH A . 
F 5 HOH   60  360 2    HOH   HOH A . 
F 5 HOH   61  361 169  HOH   HOH A . 
F 5 HOH   62  362 662  HOH   HOH A . 
F 5 HOH   63  363 66   HOH   HOH A . 
F 5 HOH   64  364 139  HOH   HOH A . 
F 5 HOH   65  365 10   HOH   HOH A . 
F 5 HOH   66  366 1275 HOH   HOH A . 
F 5 HOH   67  367 102  HOH   HOH A . 
F 5 HOH   68  368 19   HOH   HOH A . 
F 5 HOH   69  369 396  HOH   HOH A . 
F 5 HOH   70  370 159  HOH   HOH A . 
F 5 HOH   71  371 36   HOH   HOH A . 
F 5 HOH   72  372 5    HOH   HOH A . 
F 5 HOH   73  373 115  HOH   HOH A . 
F 5 HOH   74  374 8    HOH   HOH A . 
F 5 HOH   75  375 138  HOH   HOH A . 
F 5 HOH   76  376 81   HOH   HOH A . 
F 5 HOH   77  377 218  HOH   HOH A . 
F 5 HOH   78  378 162  HOH   HOH A . 
F 5 HOH   79  379 45   HOH   HOH A . 
F 5 HOH   80  380 939  HOH   HOH A . 
F 5 HOH   81  381 26   HOH   HOH A . 
F 5 HOH   82  382 46   HOH   HOH A . 
F 5 HOH   83  383 56   HOH   HOH A . 
F 5 HOH   84  384 366  HOH   HOH A . 
F 5 HOH   85  385 186  HOH   HOH A . 
F 5 HOH   86  386 134  HOH   HOH A . 
F 5 HOH   87  387 140  HOH   HOH A . 
F 5 HOH   88  388 62   HOH   HOH A . 
F 5 HOH   89  389 154  HOH   HOH A . 
F 5 HOH   90  390 17   HOH   HOH A . 
F 5 HOH   91  391 85   HOH   HOH A . 
F 5 HOH   92  392 27   HOH   HOH A . 
F 5 HOH   93  393 49   HOH   HOH A . 
F 5 HOH   94  394 351  HOH   HOH A . 
F 5 HOH   95  395 74   HOH   HOH A . 
F 5 HOH   96  396 35   HOH   HOH A . 
F 5 HOH   97  397 58   HOH   HOH A . 
F 5 HOH   98  398 148  HOH   HOH A . 
F 5 HOH   99  399 199  HOH   HOH A . 
F 5 HOH   100 400 6    HOH   HOH A . 
F 5 HOH   101 401 116  HOH   HOH A . 
F 5 HOH   102 402 195  HOH   HOH A . 
F 5 HOH   103 403 461  HOH   HOH A . 
F 5 HOH   104 404 1094 HOH   HOH A . 
F 5 HOH   105 405 83   HOH   HOH A . 
F 5 HOH   106 406 34   HOH   HOH A . 
F 5 HOH   107 407 96   HOH   HOH A . 
F 5 HOH   108 408 1308 HOH   HOH A . 
F 5 HOH   109 409 12   HOH   HOH A . 
F 5 HOH   110 410 1310 HOH   HOH A . 
F 5 HOH   111 411 67   HOH   HOH A . 
F 5 HOH   112 412 1315 HOH   HOH A . 
F 5 HOH   113 413 25   HOH   HOH A . 
F 5 HOH   114 414 333  HOH   HOH A . 
F 5 HOH   115 415 121  HOH   HOH A . 
F 5 HOH   116 416 3    HOH   HOH A . 
F 5 HOH   117 417 1068 HOH   HOH A . 
F 5 HOH   118 418 303  HOH   HOH A . 
F 5 HOH   119 419 68   HOH   HOH A . 
F 5 HOH   120 420 123  HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 78   HOH   HOH A . 
F 5 HOH   123 423 53   HOH   HOH A . 
F 5 HOH   124 424 122  HOH   HOH A . 
F 5 HOH   125 425 95   HOH   HOH A . 
F 5 HOH   126 426 156  HOH   HOH A . 
F 5 HOH   127 427 132  HOH   HOH A . 
F 5 HOH   128 428 397  HOH   HOH A . 
F 5 HOH   129 429 51   HOH   HOH A . 
F 5 HOH   130 430 1279 HOH   HOH A . 
F 5 HOH   131 431 24   HOH   HOH A . 
F 5 HOH   132 432 7    HOH   HOH A . 
F 5 HOH   133 433 405  HOH   HOH A . 
F 5 HOH   134 434 381  HOH   HOH A . 
F 5 HOH   135 435 582  HOH   HOH A . 
F 5 HOH   136 436 4    HOH   HOH A . 
F 5 HOH   137 437 1309 HOH   HOH A . 
F 5 HOH   138 438 1222 HOH   HOH A . 
F 5 HOH   139 439 1296 HOH   HOH A . 
F 5 HOH   140 440 71   HOH   HOH A . 
F 5 HOH   141 441 212  HOH   HOH A . 
F 5 HOH   142 442 80   HOH   HOH A . 
F 5 HOH   143 443 40   HOH   HOH A . 
F 5 HOH   144 444 73   HOH   HOH A . 
F 5 HOH   145 445 1286 HOH   HOH A . 
F 5 HOH   146 446 944  HOH   HOH A . 
F 5 HOH   147 447 16   HOH   HOH A . 
F 5 HOH   148 448 94   HOH   HOH A . 
F 5 HOH   149 449 1238 HOH   HOH A . 
F 5 HOH   150 450 952  HOH   HOH A . 
F 5 HOH   151 451 188  HOH   HOH A . 
F 5 HOH   152 452 104  HOH   HOH A . 
F 5 HOH   153 453 79   HOH   HOH A . 
F 5 HOH   154 454 576  HOH   HOH A . 
F 5 HOH   155 455 1189 HOH   HOH A . 
F 5 HOH   156 456 97   HOH   HOH A . 
F 5 HOH   157 457 1119 HOH   HOH A . 
F 5 HOH   158 458 1134 HOH   HOH A . 
F 5 HOH   159 459 330  HOH   HOH A . 
F 5 HOH   160 460 1313 HOH   HOH A . 
F 5 HOH   161 461 1    HOH   HOH A . 
F 5 HOH   162 462 107  HOH   HOH A . 
F 5 HOH   163 463 509  HOH   HOH A . 
F 5 HOH   164 464 3    HOH   HOH A . 
F 5 HOH   165 465 726  HOH   HOH A . 
F 5 HOH   166 466 408  HOH   HOH A . 
F 5 HOH   167 467 163  HOH   HOH A . 
F 5 HOH   168 468 319  HOH   HOH A . 
F 5 HOH   169 469 756  HOH   HOH A . 
F 5 HOH   170 470 63   HOH   HOH A . 
F 5 HOH   171 471 556  HOH   HOH A . 
F 5 HOH   172 472 126  HOH   HOH A . 
F 5 HOH   173 473 361  HOH   HOH A . 
F 5 HOH   174 474 1276 HOH   HOH A . 
F 5 HOH   175 475 801  HOH   HOH A . 
F 5 HOH   176 476 280  HOH   HOH A . 
F 5 HOH   177 477 1307 HOH   HOH A . 
F 5 HOH   178 478 370  HOH   HOH A . 
F 5 HOH   179 479 342  HOH   HOH A . 
F 5 HOH   180 480 250  HOH   HOH A . 
F 5 HOH   181 481 224  HOH   HOH A . 
F 5 HOH   182 482 267  HOH   HOH A . 
F 5 HOH   183 483 202  HOH   HOH A . 
F 5 HOH   184 484 1306 HOH   HOH A . 
F 5 HOH   185 485 1287 HOH   HOH A . 
F 5 HOH   186 486 135  HOH   HOH A . 
F 5 HOH   187 487 695  HOH   HOH A . 
F 5 HOH   188 488 521  HOH   HOH A . 
F 5 HOH   189 489 674  HOH   HOH A . 
F 5 HOH   190 490 919  HOH   HOH A . 
F 5 HOH   191 491 13   HOH   HOH A . 
F 5 HOH   192 492 1299 HOH   HOH A . 
F 5 HOH   193 493 326  HOH   HOH A . 
F 5 HOH   194 494 318  HOH   HOH A . 
F 5 HOH   195 495 309  HOH   HOH A . 
F 5 HOH   196 496 1314 HOH   HOH A . 
F 5 HOH   197 497 331  HOH   HOH A . 
F 5 HOH   198 498 711  HOH   HOH A . 
F 5 HOH   199 499 805  HOH   HOH A . 
F 5 HOH   200 500 941  HOH   HOH A . 
F 5 HOH   201 501 315  HOH   HOH A . 
F 5 HOH   202 502 263  HOH   HOH A . 
F 5 HOH   203 503 208  HOH   HOH A . 
F 5 HOH   204 504 152  HOH   HOH A . 
F 5 HOH   205 505 356  HOH   HOH A . 
F 5 HOH   206 506 1071 HOH   HOH A . 
F 5 HOH   207 507 1284 HOH   HOH A . 
F 5 HOH   208 508 12   HOH   HOH A . 
F 5 HOH   209 509 180  HOH   HOH A . 
F 5 HOH   210 510 363  HOH   HOH A . 
F 5 HOH   211 511 14   HOH   HOH A . 
F 5 HOH   212 512 313  HOH   HOH A . 
F 5 HOH   213 513 4    HOH   HOH A . 
F 5 HOH   214 514 371  HOH   HOH A . 
F 5 HOH   215 515 16   HOH   HOH A . 
F 5 HOH   216 516 185  HOH   HOH A . 
F 5 HOH   217 517 429  HOH   HOH A . 
F 5 HOH   218 518 70   HOH   HOH A . 
F 5 HOH   219 519 376  HOH   HOH A . 
F 5 HOH   220 520 772  HOH   HOH A . 
F 5 HOH   221 521 1074 HOH   HOH A . 
F 5 HOH   222 522 6    HOH   HOH A . 
F 5 HOH   223 523 346  HOH   HOH A . 
F 5 HOH   224 524 1292 HOH   HOH A . 
F 5 HOH   225 525 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 364  HOH   HOH B . 
G 5 HOH   5   205 398  HOH   HOH B . 
G 5 HOH   6   206 1249 HOH   HOH B . 
G 5 HOH   7   207 358  HOH   HOH B . 
G 5 HOH   8   208 900  HOH   HOH B . 
G 5 HOH   9   209 205  HOH   HOH B . 
G 5 HOH   10  210 758  HOH   HOH B . 
G 5 HOH   11  211 654  HOH   HOH B . 
G 5 HOH   12  212 120  HOH   HOH B . 
G 5 HOH   13  213 531  HOH   HOH B . 
G 5 HOH   14  214 50   HOH   HOH B . 
G 5 HOH   15  215 332  HOH   HOH B . 
G 5 HOH   16  216 743  HOH   HOH B . 
G 5 HOH   17  217 353  HOH   HOH B . 
G 5 HOH   18  218 264  HOH   HOH B . 
G 5 HOH   19  219 452  HOH   HOH B . 
G 5 HOH   20  220 232  HOH   HOH B . 
G 5 HOH   21  221 1278 HOH   HOH B . 
G 5 HOH   22  222 444  HOH   HOH B . 
G 5 HOH   23  223 1140 HOH   HOH B . 
G 5 HOH   24  224 343  HOH   HOH B . 
G 5 HOH   25  225 172  HOH   HOH B . 
G 5 HOH   26  226 131  HOH   HOH B . 
G 5 HOH   27  227 54   HOH   HOH B . 
G 5 HOH   28  228 82   HOH   HOH B . 
G 5 HOH   29  229 282  HOH   HOH B . 
G 5 HOH   30  230 60   HOH   HOH B . 
G 5 HOH   31  231 75   HOH   HOH B . 
G 5 HOH   32  232 325  HOH   HOH B . 
G 5 HOH   33  233 1312 HOH   HOH B . 
G 5 HOH   34  234 127  HOH   HOH B . 
G 5 HOH   35  235 300  HOH   HOH B . 
G 5 HOH   36  236 69   HOH   HOH B . 
G 5 HOH   37  237 166  HOH   HOH B . 
G 5 HOH   38  238 723  HOH   HOH B . 
G 5 HOH   39  239 276  HOH   HOH B . 
G 5 HOH   40  240 128  HOH   HOH B . 
G 5 HOH   41  241 110  HOH   HOH B . 
G 5 HOH   42  242 133  HOH   HOH B . 
G 5 HOH   43  243 272  HOH   HOH B . 
G 5 HOH   44  244 14   HOH   HOH B . 
G 5 HOH   45  245 1    HOH   HOH B . 
G 5 HOH   46  246 30   HOH   HOH B . 
G 5 HOH   47  247 9    HOH   HOH B . 
G 5 HOH   48  248 231  HOH   HOH B . 
G 5 HOH   49  249 181  HOH   HOH B . 
G 5 HOH   50  250 129  HOH   HOH B . 
G 5 HOH   51  251 144  HOH   HOH B . 
G 5 HOH   52  252 41   HOH   HOH B . 
G 5 HOH   53  253 52   HOH   HOH B . 
G 5 HOH   54  254 31   HOH   HOH B . 
G 5 HOH   55  255 252  HOH   HOH B . 
G 5 HOH   56  256 150  HOH   HOH B . 
G 5 HOH   57  257 72   HOH   HOH B . 
G 5 HOH   58  258 103  HOH   HOH B . 
G 5 HOH   59  259 347  HOH   HOH B . 
G 5 HOH   60  260 47   HOH   HOH B . 
G 5 HOH   61  261 302  HOH   HOH B . 
G 5 HOH   62  262 143  HOH   HOH B . 
G 5 HOH   63  263 221  HOH   HOH B . 
G 5 HOH   64  264 391  HOH   HOH B . 
G 5 HOH   65  265 10   HOH   HOH B . 
G 5 HOH   66  266 242  HOH   HOH B . 
G 5 HOH   67  267 59   HOH   HOH B . 
G 5 HOH   68  268 61   HOH   HOH B . 
G 5 HOH   69  269 11   HOH   HOH B . 
G 5 HOH   70  270 117  HOH   HOH B . 
G 5 HOH   71  271 147  HOH   HOH B . 
G 5 HOH   72  272 271  HOH   HOH B . 
G 5 HOH   73  273 243  HOH   HOH B . 
G 5 HOH   74  274 77   HOH   HOH B . 
G 5 HOH   75  275 20   HOH   HOH B . 
G 5 HOH   76  276 114  HOH   HOH B . 
G 5 HOH   77  277 287  HOH   HOH B . 
G 5 HOH   78  278 84   HOH   HOH B . 
G 5 HOH   79  279 1277 HOH   HOH B . 
G 5 HOH   80  280 175  HOH   HOH B . 
G 5 HOH   81  281 216  HOH   HOH B . 
G 5 HOH   82  282 43   HOH   HOH B . 
G 5 HOH   83  283 1305 HOH   HOH B . 
G 5 HOH   84  284 235  HOH   HOH B . 
G 5 HOH   85  285 22   HOH   HOH B . 
G 5 HOH   86  286 416  HOH   HOH B . 
G 5 HOH   87  287 1106 HOH   HOH B . 
G 5 HOH   88  288 13   HOH   HOH B . 
G 5 HOH   89  289 106  HOH   HOH B . 
G 5 HOH   90  290 88   HOH   HOH B . 
G 5 HOH   91  291 1066 HOH   HOH B . 
G 5 HOH   92  292 220  HOH   HOH B . 
G 5 HOH   93  293 89   HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 99   HOH   HOH B . 
G 5 HOH   96  296 311  HOH   HOH B . 
G 5 HOH   97  297 112  HOH   HOH B . 
G 5 HOH   98  298 160  HOH   HOH B . 
G 5 HOH   99  299 299  HOH   HOH B . 
G 5 HOH   100 300 142  HOH   HOH B . 
G 5 HOH   101 301 215  HOH   HOH B . 
G 5 HOH   102 302 387  HOH   HOH B . 
G 5 HOH   103 303 297  HOH   HOH B . 
G 5 HOH   104 304 316  HOH   HOH B . 
G 5 HOH   105 305 118  HOH   HOH B . 
G 5 HOH   106 306 32   HOH   HOH B . 
G 5 HOH   107 307 1285 HOH   HOH B . 
G 5 HOH   108 308 1274 HOH   HOH B . 
G 5 HOH   109 309 101  HOH   HOH B . 
G 5 HOH   110 310 170  HOH   HOH B . 
G 5 HOH   111 311 38   HOH   HOH B . 
G 5 HOH   112 312 48   HOH   HOH B . 
G 5 HOH   113 313 37   HOH   HOH B . 
G 5 HOH   114 314 91   HOH   HOH B . 
G 5 HOH   115 315 177  HOH   HOH B . 
G 5 HOH   116 316 704  HOH   HOH B . 
G 5 HOH   117 317 23   HOH   HOH B . 
G 5 HOH   118 318 197  HOH   HOH B . 
G 5 HOH   119 319 28   HOH   HOH B . 
G 5 HOH   120 320 44   HOH   HOH B . 
G 5 HOH   121 321 635  HOH   HOH B . 
G 5 HOH   122 322 182  HOH   HOH B . 
G 5 HOH   123 323 100  HOH   HOH B . 
G 5 HOH   124 324 29   HOH   HOH B . 
G 5 HOH   125 325 207  HOH   HOH B . 
G 5 HOH   126 326 161  HOH   HOH B . 
G 5 HOH   127 327 341  HOH   HOH B . 
G 5 HOH   128 328 1294 HOH   HOH B . 
G 5 HOH   129 329 141  HOH   HOH B . 
G 5 HOH   130 330 1291 HOH   HOH B . 
G 5 HOH   131 331 55   HOH   HOH B . 
G 5 HOH   132 332 98   HOH   HOH B . 
G 5 HOH   133 333 717  HOH   HOH B . 
G 5 HOH   134 334 334  HOH   HOH B . 
G 5 HOH   135 335 1126 HOH   HOH B . 
G 5 HOH   136 336 445  HOH   HOH B . 
G 5 HOH   137 337 65   HOH   HOH B . 
G 5 HOH   138 338 234  HOH   HOH B . 
G 5 HOH   139 339 619  HOH   HOH B . 
G 5 HOH   140 340 1293 HOH   HOH B . 
G 5 HOH   141 341 960  HOH   HOH B . 
G 5 HOH   142 342 178  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 339  HOH   HOH B . 
G 5 HOH   145 345 90   HOH   HOH B . 
G 5 HOH   146 346 87   HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 1304 HOH   HOH B . 
G 5 HOH   149 349 1046 HOH   HOH B . 
G 5 HOH   150 350 623  HOH   HOH B . 
G 5 HOH   151 351 335  HOH   HOH B . 
G 5 HOH   152 352 191  HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 290  HOH   HOH B . 
G 5 HOH   156 356 541  HOH   HOH B . 
G 5 HOH   157 357 203  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 718  HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 479  HOH   HOH B . 
G 5 HOH   164 364 291  HOH   HOH B . 
G 5 HOH   165 365 1316 HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 373  HOH   HOH B . 
G 5 HOH   168 368 615  HOH   HOH B . 
G 5 HOH   169 369 340  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 1303 HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 431  HOH   HOH B . 
G 5 HOH   175 375 1173 HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 1163 HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 981  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 265  HOH   HOH B . 
G 5 HOH   187 387 1298 HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 470  HOH   HOH B . 
G 5 HOH   190 390 350  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  HOH   HOH B . 
G 5 HOH   195 395 314  HOH   HOH B . 
G 5 HOH   196 396 274  HOH   HOH B . 
G 5 HOH   197 397 566  HOH   HOH B . 
G 5 HOH   198 398 157  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 792  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HD0 
_cell.length_a           88.804 
_cell.length_b           88.804 
_cell.length_c           39.478 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HD0 
_symmetry.space_group_name_H-M             'P 43' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HD0 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.64 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HD0 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156134 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.039 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.400 
_reflns.B_iso_Wilson_estimate        12.000 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.042 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1013718 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.020 1.040  ? 42273 7488 ? 1.115 ? ? ? 5.600 ? 1.200  ? ? ? ? ? ? 97.100 1.230 0.507 0.773 ? 
1 2 5.590 44.400 ? 7143  1038 ? 0.025 ? ? ? 6.900 ? 64.200 ? ? ? ? ? ? 99.900 0.027 0.010 1.000 ? 
# 
_refine.entry_id                                 7HD0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7300 
_refine.ls_number_reflns_obs                     156043 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1452 
_refine.ls_R_factor_R_work                       0.1446 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1580 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7521 
_refine.ls_number_reflns_R_work                  148522 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.3207 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.0900 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                69.320 
_refine.B_iso_min                                9.060 
_refine.pdbx_overall_phase_error                 17.6200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3008 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.77 
_refine_hist.pdbx_B_iso_mean_solvent          30.64 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0200 1.0300  30 95.0000  4751 . 0.3383 0.3198 . 191 0.0000 4942 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 4935 . 0.2897 0.2685 . 279 0.0000 5214 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 4880 . 0.2497 0.2505 . 277 0.0000 5157 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 4921 . 0.2401 0.2494 . 280 0.0000 5201 . 'X-RAY DIFFRACTION' . 
1.0700 1.0800  30 100.0000 4898 . 0.2300 0.2498 . 235 0.0000 5133 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 4958 . 0.2065 0.2286 . 236 0.0000 5194 . 'X-RAY DIFFRACTION' . 
1.1000 1.1100  30 100.0000 4896 . 0.1886 0.1953 . 269 0.0000 5165 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5004 . 0.1790 0.1938 . 218 0.0000 5222 . 'X-RAY DIFFRACTION' . 
1.1300 1.1500  30 100.0000 4919 . 0.1627 0.1778 . 240 0.0000 5159 . 'X-RAY DIFFRACTION' . 
1.1500 1.1700  30 100.0000 4945 . 0.1511 0.1682 . 260 0.0000 5205 . 'X-RAY DIFFRACTION' . 
1.1700 1.1900  30 100.0000 4937 . 0.1412 0.1610 . 250 0.0000 5187 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 4858 . 0.1329 0.1609 . 265 0.0000 5123 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5047 . 0.1275 0.1487 . 223 0.0000 5270 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 4919 . 0.1293 0.1459 . 245 0.0000 5164 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 4930 . 0.1302 0.1483 . 251 0.0000 5181 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 4941 . 0.1312 0.1469 . 267 0.0000 5208 . 'X-RAY DIFFRACTION' . 
1.3200 1.3500  30 100.0000 4945 . 0.1364 0.1506 . 252 0.0000 5197 . 'X-RAY DIFFRACTION' . 
1.3500 1.3800  30 100.0000 4957 . 0.1361 0.1627 . 253 0.0000 5210 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 100.0000 4965 . 0.1329 0.1612 . 240 0.0000 5205 . 'X-RAY DIFFRACTION' . 
1.4300 1.4700  30 100.0000 4952 . 0.1289 0.1439 . 246 0.0000 5198 . 'X-RAY DIFFRACTION' . 
1.4700 1.5200  30 100.0000 4986 . 0.1205 0.1308 . 239 0.0000 5225 . 'X-RAY DIFFRACTION' . 
1.5200 1.5900  30 100.0000 4943 . 0.1208 0.1325 . 263 0.0000 5206 . 'X-RAY DIFFRACTION' . 
1.5900 1.6600  30 100.0000 4949 . 0.1219 0.1361 . 263 0.0000 5212 . 'X-RAY DIFFRACTION' . 
1.6600 1.7400  30 100.0000 5032 . 0.1299 0.1457 . 204 0.0000 5236 . 'X-RAY DIFFRACTION' . 
1.7400 1.8500  30 100.0000 4942 . 0.1344 0.1412 . 292 0.0000 5234 . 'X-RAY DIFFRACTION' . 
1.8500 2.0000  30 100.0000 4978 . 0.1342 0.1377 . 242 0.0000 5220 . 'X-RAY DIFFRACTION' . 
2.0000 2.2000  30 100.0000 4946 . 0.1380 0.1396 . 287 0.0000 5233 . 'X-RAY DIFFRACTION' . 
2.2000 2.5200  30 100.0000 5003 . 0.1382 0.1427 . 254 0.0000 5257 . 'X-RAY DIFFRACTION' . 
2.5200 3.1700  30 100.0000 5019 . 0.1494 0.1652 . 248 0.0000 5267 . 'X-RAY DIFFRACTION' . 
3.1700 44.4000 30 100.0000 5166 . 0.1481 0.1732 . 252 0.0000 5418 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HD0 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003703' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD0 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HD0 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD0 B 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HD0 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD0 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD0 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD0 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HD0 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    167 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.42   -133.23 
2 1 SER A 128 ? B 73.36   -6.42   
3 1 PHE A 168 ? B -137.52 -55.13  
4 1 HIS B 86  ? ? 58.27   -128.24 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O B A HOH 522 ? 5.83 . 
2 1 O ? A HOH 523 ? 5.91 . 
3 1 O ? A HOH 524 ? 5.92 . 
4 1 O ? A HOH 525 ? 7.61 . 
5 1 O ? B HOH 401 ? 6.53 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A6Y N2   N  N N 1   
A1A6Y C3   C  N N 2   
A1A6Y C6   C  Y N 3   
A1A6Y C9   C  Y N 4   
A1A6Y C12  C  Y N 5   
A1A6Y C1   C  N N 6   
A1A6Y C10  C  Y N 7   
A1A6Y C11  C  Y N 8   
A1A6Y C2   C  N S 9   
A1A6Y C4   C  Y N 10  
A1A6Y C5   C  Y N 11  
A1A6Y C7   C  Y N 12  
A1A6Y C8   C  Y N 13  
A1A6Y N1   N  Y N 14  
A1A6Y N3   N  Y N 15  
A1A6Y N4   N  Y N 16  
A1A6Y N5   N  Y N 17  
A1A6Y O1   O  N N 18  
A1A6Y S1   S  Y N 19  
A1A6Y H9   H  N N 20  
A1A6Y H6   H  N N 21  
A1A6Y H5   H  N N 22  
A1A6Y H8   H  N N 23  
A1A6Y H12  H  N N 24  
A1A6Y H3   H  N N 25  
A1A6Y H4   H  N N 26  
A1A6Y H11  H  N N 27  
A1A6Y H1   H  N N 28  
A1A6Y H7   H  N N 29  
A1A6Y H10  H  N N 30  
A1A6Y H13  H  N N 31  
A1A6Y H2   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CL    CL   CL N N 106 
CYS   N    N  N N 107 
CYS   CA   C  N R 108 
CYS   C    C  N N 109 
CYS   O    O  N N 110 
CYS   CB   C  N N 111 
CYS   SG   S  N N 112 
CYS   OXT  O  N N 113 
CYS   H    H  N N 114 
CYS   H2   H  N N 115 
CYS   HA   H  N N 116 
CYS   HB2  H  N N 117 
CYS   HB3  H  N N 118 
CYS   HG   H  N N 119 
CYS   HXT  H  N N 120 
GLN   N    N  N N 121 
GLN   CA   C  N S 122 
GLN   C    C  N N 123 
GLN   O    O  N N 124 
GLN   CB   C  N N 125 
GLN   CG   C  N N 126 
GLN   CD   C  N N 127 
GLN   OE1  O  N N 128 
GLN   NE2  N  N N 129 
GLN   OXT  O  N N 130 
GLN   H    H  N N 131 
GLN   H2   H  N N 132 
GLN   HA   H  N N 133 
GLN   HB2  H  N N 134 
GLN   HB3  H  N N 135 
GLN   HG2  H  N N 136 
GLN   HG3  H  N N 137 
GLN   HE21 H  N N 138 
GLN   HE22 H  N N 139 
GLN   HXT  H  N N 140 
GLU   N    N  N N 141 
GLU   CA   C  N S 142 
GLU   C    C  N N 143 
GLU   O    O  N N 144 
GLU   CB   C  N N 145 
GLU   CG   C  N N 146 
GLU   CD   C  N N 147 
GLU   OE1  O  N N 148 
GLU   OE2  O  N N 149 
GLU   OXT  O  N N 150 
GLU   H    H  N N 151 
GLU   H2   H  N N 152 
GLU   HA   H  N N 153 
GLU   HB2  H  N N 154 
GLU   HB3  H  N N 155 
GLU   HG2  H  N N 156 
GLU   HG3  H  N N 157 
GLU   HE2  H  N N 158 
GLU   HXT  H  N N 159 
GLY   N    N  N N 160 
GLY   CA   C  N N 161 
GLY   C    C  N N 162 
GLY   O    O  N N 163 
GLY   OXT  O  N N 164 
GLY   H    H  N N 165 
GLY   H2   H  N N 166 
GLY   HA2  H  N N 167 
GLY   HA3  H  N N 168 
GLY   HXT  H  N N 169 
HIS   N    N  N N 170 
HIS   CA   C  N S 171 
HIS   C    C  N N 172 
HIS   O    O  N N 173 
HIS   CB   C  N N 174 
HIS   CG   C  Y N 175 
HIS   ND1  N  Y N 176 
HIS   CD2  C  Y N 177 
HIS   CE1  C  Y N 178 
HIS   NE2  N  Y N 179 
HIS   OXT  O  N N 180 
HIS   H    H  N N 181 
HIS   H2   H  N N 182 
HIS   HA   H  N N 183 
HIS   HB2  H  N N 184 
HIS   HB3  H  N N 185 
HIS   HD1  H  N N 186 
HIS   HD2  H  N N 187 
HIS   HE1  H  N N 188 
HIS   HE2  H  N N 189 
HIS   HXT  H  N N 190 
HOH   O    O  N N 191 
HOH   H1   H  N N 192 
HOH   H2   H  N N 193 
ILE   N    N  N N 194 
ILE   CA   C  N S 195 
ILE   C    C  N N 196 
ILE   O    O  N N 197 
ILE   CB   C  N S 198 
ILE   CG1  C  N N 199 
ILE   CG2  C  N N 200 
ILE   CD1  C  N N 201 
ILE   OXT  O  N N 202 
ILE   H    H  N N 203 
ILE   H2   H  N N 204 
ILE   HA   H  N N 205 
ILE   HB   H  N N 206 
ILE   HG12 H  N N 207 
ILE   HG13 H  N N 208 
ILE   HG21 H  N N 209 
ILE   HG22 H  N N 210 
ILE   HG23 H  N N 211 
ILE   HD11 H  N N 212 
ILE   HD12 H  N N 213 
ILE   HD13 H  N N 214 
ILE   HXT  H  N N 215 
LEU   N    N  N N 216 
LEU   CA   C  N S 217 
LEU   C    C  N N 218 
LEU   O    O  N N 219 
LEU   CB   C  N N 220 
LEU   CG   C  N N 221 
LEU   CD1  C  N N 222 
LEU   CD2  C  N N 223 
LEU   OXT  O  N N 224 
LEU   H    H  N N 225 
LEU   H2   H  N N 226 
LEU   HA   H  N N 227 
LEU   HB2  H  N N 228 
LEU   HB3  H  N N 229 
LEU   HG   H  N N 230 
LEU   HD11 H  N N 231 
LEU   HD12 H  N N 232 
LEU   HD13 H  N N 233 
LEU   HD21 H  N N 234 
LEU   HD22 H  N N 235 
LEU   HD23 H  N N 236 
LEU   HXT  H  N N 237 
LYS   N    N  N N 238 
LYS   CA   C  N S 239 
LYS   C    C  N N 240 
LYS   O    O  N N 241 
LYS   CB   C  N N 242 
LYS   CG   C  N N 243 
LYS   CD   C  N N 244 
LYS   CE   C  N N 245 
LYS   NZ   N  N N 246 
LYS   OXT  O  N N 247 
LYS   H    H  N N 248 
LYS   H2   H  N N 249 
LYS   HA   H  N N 250 
LYS   HB2  H  N N 251 
LYS   HB3  H  N N 252 
LYS   HG2  H  N N 253 
LYS   HG3  H  N N 254 
LYS   HD2  H  N N 255 
LYS   HD3  H  N N 256 
LYS   HE2  H  N N 257 
LYS   HE3  H  N N 258 
LYS   HZ1  H  N N 259 
LYS   HZ2  H  N N 260 
LYS   HZ3  H  N N 261 
LYS   HXT  H  N N 262 
MET   N    N  N N 263 
MET   CA   C  N S 264 
MET   C    C  N N 265 
MET   O    O  N N 266 
MET   CB   C  N N 267 
MET   CG   C  N N 268 
MET   SD   S  N N 269 
MET   CE   C  N N 270 
MET   OXT  O  N N 271 
MET   H    H  N N 272 
MET   H2   H  N N 273 
MET   HA   H  N N 274 
MET   HB2  H  N N 275 
MET   HB3  H  N N 276 
MET   HG2  H  N N 277 
MET   HG3  H  N N 278 
MET   HE1  H  N N 279 
MET   HE2  H  N N 280 
MET   HE3  H  N N 281 
MET   HXT  H  N N 282 
PHE   N    N  N N 283 
PHE   CA   C  N S 284 
PHE   C    C  N N 285 
PHE   O    O  N N 286 
PHE   CB   C  N N 287 
PHE   CG   C  Y N 288 
PHE   CD1  C  Y N 289 
PHE   CD2  C  Y N 290 
PHE   CE1  C  Y N 291 
PHE   CE2  C  Y N 292 
PHE   CZ   C  Y N 293 
PHE   OXT  O  N N 294 
PHE   H    H  N N 295 
PHE   H2   H  N N 296 
PHE   HA   H  N N 297 
PHE   HB2  H  N N 298 
PHE   HB3  H  N N 299 
PHE   HD1  H  N N 300 
PHE   HD2  H  N N 301 
PHE   HE1  H  N N 302 
PHE   HE2  H  N N 303 
PHE   HZ   H  N N 304 
PHE   HXT  H  N N 305 
PRO   N    N  N N 306 
PRO   CA   C  N S 307 
PRO   C    C  N N 308 
PRO   O    O  N N 309 
PRO   CB   C  N N 310 
PRO   CG   C  N N 311 
PRO   CD   C  N N 312 
PRO   OXT  O  N N 313 
PRO   H    H  N N 314 
PRO   HA   H  N N 315 
PRO   HB2  H  N N 316 
PRO   HB3  H  N N 317 
PRO   HG2  H  N N 318 
PRO   HG3  H  N N 319 
PRO   HD2  H  N N 320 
PRO   HD3  H  N N 321 
PRO   HXT  H  N N 322 
SER   N    N  N N 323 
SER   CA   C  N S 324 
SER   C    C  N N 325 
SER   O    O  N N 326 
SER   CB   C  N N 327 
SER   OG   O  N N 328 
SER   OXT  O  N N 329 
SER   H    H  N N 330 
SER   H2   H  N N 331 
SER   HA   H  N N 332 
SER   HB2  H  N N 333 
SER   HB3  H  N N 334 
SER   HG   H  N N 335 
SER   HXT  H  N N 336 
TFA   C1   C  N N 337 
TFA   C2   C  N N 338 
TFA   O    O  N N 339 
TFA   F1   F  N N 340 
TFA   F2   F  N N 341 
TFA   F3   F  N N 342 
TFA   OXT  O  N N 343 
TFA   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TYR   N    N  N N 362 
TYR   CA   C  N S 363 
TYR   C    C  N N 364 
TYR   O    O  N N 365 
TYR   CB   C  N N 366 
TYR   CG   C  Y N 367 
TYR   CD1  C  Y N 368 
TYR   CD2  C  Y N 369 
TYR   CE1  C  Y N 370 
TYR   CE2  C  Y N 371 
TYR   CZ   C  Y N 372 
TYR   OH   O  N N 373 
TYR   OXT  O  N N 374 
TYR   H    H  N N 375 
TYR   H2   H  N N 376 
TYR   HA   H  N N 377 
TYR   HB2  H  N N 378 
TYR   HB3  H  N N 379 
TYR   HD1  H  N N 380 
TYR   HD2  H  N N 381 
TYR   HE1  H  N N 382 
TYR   HE2  H  N N 383 
TYR   HH   H  N N 384 
TYR   HXT  H  N N 385 
VAL   N    N  N N 386 
VAL   CA   C  N S 387 
VAL   C    C  N N 388 
VAL   O    O  N N 389 
VAL   CB   C  N N 390 
VAL   CG1  C  N N 391 
VAL   CG2  C  N N 392 
VAL   OXT  O  N N 393 
VAL   H    H  N N 394 
VAL   H2   H  N N 395 
VAL   HA   H  N N 396 
VAL   HB   H  N N 397 
VAL   HG11 H  N N 398 
VAL   HG12 H  N N 399 
VAL   HG13 H  N N 400 
VAL   HG21 H  N N 401 
VAL   HG22 H  N N 402 
VAL   HG23 H  N N 403 
VAL   HXT  H  N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A6Y C5  N1   sing Y N 1   
A1A6Y C5  C4   doub Y N 2   
A1A6Y N1  C6   doub Y N 3   
A1A6Y C3  C4   sing N N 4   
A1A6Y C3  C2   sing N N 5   
A1A6Y C4  S1   sing Y N 6   
A1A6Y C6  S1   sing Y N 7   
A1A6Y O1  C1   sing N N 8   
A1A6Y C1  C2   sing N N 9   
A1A6Y C2  N2   sing N N 10  
A1A6Y N2  C7   sing N N 11  
A1A6Y C7  C10  doub Y N 12  
A1A6Y C7  N3   sing Y N 13  
A1A6Y C11 C10  sing Y N 14  
A1A6Y C11 C12  doub Y N 15  
A1A6Y C10 C9   sing Y N 16  
A1A6Y N3  C8   doub Y N 17  
A1A6Y C12 N5   sing Y N 18  
A1A6Y C8  N4   sing Y N 19  
A1A6Y C9  N5   sing Y N 20  
A1A6Y C9  N4   doub Y N 21  
A1A6Y N2  H9   sing N N 22  
A1A6Y C3  H6   sing N N 23  
A1A6Y C3  H5   sing N N 24  
A1A6Y C6  H8   sing N N 25  
A1A6Y C12 H12  sing N N 26  
A1A6Y C1  H3   sing N N 27  
A1A6Y C1  H4   sing N N 28  
A1A6Y C11 H11  sing N N 29  
A1A6Y C2  H1   sing N N 30  
A1A6Y C5  H7   sing N N 31  
A1A6Y C8  H10  sing N N 32  
A1A6Y N5  H13  sing N N 33  
A1A6Y O1  H2   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
CYS   N   CA   sing N N 104 
CYS   N   H    sing N N 105 
CYS   N   H2   sing N N 106 
CYS   CA  C    sing N N 107 
CYS   CA  CB   sing N N 108 
CYS   CA  HA   sing N N 109 
CYS   C   O    doub N N 110 
CYS   C   OXT  sing N N 111 
CYS   CB  SG   sing N N 112 
CYS   CB  HB2  sing N N 113 
CYS   CB  HB3  sing N N 114 
CYS   SG  HG   sing N N 115 
CYS   OXT HXT  sing N N 116 
GLN   N   CA   sing N N 117 
GLN   N   H    sing N N 118 
GLN   N   H2   sing N N 119 
GLN   CA  C    sing N N 120 
GLN   CA  CB   sing N N 121 
GLN   CA  HA   sing N N 122 
GLN   C   O    doub N N 123 
GLN   C   OXT  sing N N 124 
GLN   CB  CG   sing N N 125 
GLN   CB  HB2  sing N N 126 
GLN   CB  HB3  sing N N 127 
GLN   CG  CD   sing N N 128 
GLN   CG  HG2  sing N N 129 
GLN   CG  HG3  sing N N 130 
GLN   CD  OE1  doub N N 131 
GLN   CD  NE2  sing N N 132 
GLN   NE2 HE21 sing N N 133 
GLN   NE2 HE22 sing N N 134 
GLN   OXT HXT  sing N N 135 
GLU   N   CA   sing N N 136 
GLU   N   H    sing N N 137 
GLU   N   H2   sing N N 138 
GLU   CA  C    sing N N 139 
GLU   CA  CB   sing N N 140 
GLU   CA  HA   sing N N 141 
GLU   C   O    doub N N 142 
GLU   C   OXT  sing N N 143 
GLU   CB  CG   sing N N 144 
GLU   CB  HB2  sing N N 145 
GLU   CB  HB3  sing N N 146 
GLU   CG  CD   sing N N 147 
GLU   CG  HG2  sing N N 148 
GLU   CG  HG3  sing N N 149 
GLU   CD  OE1  doub N N 150 
GLU   CD  OE2  sing N N 151 
GLU   OE2 HE2  sing N N 152 
GLU   OXT HXT  sing N N 153 
GLY   N   CA   sing N N 154 
GLY   N   H    sing N N 155 
GLY   N   H2   sing N N 156 
GLY   CA  C    sing N N 157 
GLY   CA  HA2  sing N N 158 
GLY   CA  HA3  sing N N 159 
GLY   C   O    doub N N 160 
GLY   C   OXT  sing N N 161 
GLY   OXT HXT  sing N N 162 
HIS   N   CA   sing N N 163 
HIS   N   H    sing N N 164 
HIS   N   H2   sing N N 165 
HIS   CA  C    sing N N 166 
HIS   CA  CB   sing N N 167 
HIS   CA  HA   sing N N 168 
HIS   C   O    doub N N 169 
HIS   C   OXT  sing N N 170 
HIS   CB  CG   sing N N 171 
HIS   CB  HB2  sing N N 172 
HIS   CB  HB3  sing N N 173 
HIS   CG  ND1  sing Y N 174 
HIS   CG  CD2  doub Y N 175 
HIS   ND1 CE1  doub Y N 176 
HIS   ND1 HD1  sing N N 177 
HIS   CD2 NE2  sing Y N 178 
HIS   CD2 HD2  sing N N 179 
HIS   CE1 NE2  sing Y N 180 
HIS   CE1 HE1  sing N N 181 
HIS   NE2 HE2  sing N N 182 
HIS   OXT HXT  sing N N 183 
HOH   O   H1   sing N N 184 
HOH   O   H2   sing N N 185 
ILE   N   CA   sing N N 186 
ILE   N   H    sing N N 187 
ILE   N   H2   sing N N 188 
ILE   CA  C    sing N N 189 
ILE   CA  CB   sing N N 190 
ILE   CA  HA   sing N N 191 
ILE   C   O    doub N N 192 
ILE   C   OXT  sing N N 193 
ILE   CB  CG1  sing N N 194 
ILE   CB  CG2  sing N N 195 
ILE   CB  HB   sing N N 196 
ILE   CG1 CD1  sing N N 197 
ILE   CG1 HG12 sing N N 198 
ILE   CG1 HG13 sing N N 199 
ILE   CG2 HG21 sing N N 200 
ILE   CG2 HG22 sing N N 201 
ILE   CG2 HG23 sing N N 202 
ILE   CD1 HD11 sing N N 203 
ILE   CD1 HD12 sing N N 204 
ILE   CD1 HD13 sing N N 205 
ILE   OXT HXT  sing N N 206 
LEU   N   CA   sing N N 207 
LEU   N   H    sing N N 208 
LEU   N   H2   sing N N 209 
LEU   CA  C    sing N N 210 
LEU   CA  CB   sing N N 211 
LEU   CA  HA   sing N N 212 
LEU   C   O    doub N N 213 
LEU   C   OXT  sing N N 214 
LEU   CB  CG   sing N N 215 
LEU   CB  HB2  sing N N 216 
LEU   CB  HB3  sing N N 217 
LEU   CG  CD1  sing N N 218 
LEU   CG  CD2  sing N N 219 
LEU   CG  HG   sing N N 220 
LEU   CD1 HD11 sing N N 221 
LEU   CD1 HD12 sing N N 222 
LEU   CD1 HD13 sing N N 223 
LEU   CD2 HD21 sing N N 224 
LEU   CD2 HD22 sing N N 225 
LEU   CD2 HD23 sing N N 226 
LEU   OXT HXT  sing N N 227 
LYS   N   CA   sing N N 228 
LYS   N   H    sing N N 229 
LYS   N   H2   sing N N 230 
LYS   CA  C    sing N N 231 
LYS   CA  CB   sing N N 232 
LYS   CA  HA   sing N N 233 
LYS   C   O    doub N N 234 
LYS   C   OXT  sing N N 235 
LYS   CB  CG   sing N N 236 
LYS   CB  HB2  sing N N 237 
LYS   CB  HB3  sing N N 238 
LYS   CG  CD   sing N N 239 
LYS   CG  HG2  sing N N 240 
LYS   CG  HG3  sing N N 241 
LYS   CD  CE   sing N N 242 
LYS   CD  HD2  sing N N 243 
LYS   CD  HD3  sing N N 244 
LYS   CE  NZ   sing N N 245 
LYS   CE  HE2  sing N N 246 
LYS   CE  HE3  sing N N 247 
LYS   NZ  HZ1  sing N N 248 
LYS   NZ  HZ2  sing N N 249 
LYS   NZ  HZ3  sing N N 250 
LYS   OXT HXT  sing N N 251 
MET   N   CA   sing N N 252 
MET   N   H    sing N N 253 
MET   N   H2   sing N N 254 
MET   CA  C    sing N N 255 
MET   CA  CB   sing N N 256 
MET   CA  HA   sing N N 257 
MET   C   O    doub N N 258 
MET   C   OXT  sing N N 259 
MET   CB  CG   sing N N 260 
MET   CB  HB2  sing N N 261 
MET   CB  HB3  sing N N 262 
MET   CG  SD   sing N N 263 
MET   CG  HG2  sing N N 264 
MET   CG  HG3  sing N N 265 
MET   SD  CE   sing N N 266 
MET   CE  HE1  sing N N 267 
MET   CE  HE2  sing N N 268 
MET   CE  HE3  sing N N 269 
MET   OXT HXT  sing N N 270 
PHE   N   CA   sing N N 271 
PHE   N   H    sing N N 272 
PHE   N   H2   sing N N 273 
PHE   CA  C    sing N N 274 
PHE   CA  CB   sing N N 275 
PHE   CA  HA   sing N N 276 
PHE   C   O    doub N N 277 
PHE   C   OXT  sing N N 278 
PHE   CB  CG   sing N N 279 
PHE   CB  HB2  sing N N 280 
PHE   CB  HB3  sing N N 281 
PHE   CG  CD1  doub Y N 282 
PHE   CG  CD2  sing Y N 283 
PHE   CD1 CE1  sing Y N 284 
PHE   CD1 HD1  sing N N 285 
PHE   CD2 CE2  doub Y N 286 
PHE   CD2 HD2  sing N N 287 
PHE   CE1 CZ   doub Y N 288 
PHE   CE1 HE1  sing N N 289 
PHE   CE2 CZ   sing Y N 290 
PHE   CE2 HE2  sing N N 291 
PHE   CZ  HZ   sing N N 292 
PHE   OXT HXT  sing N N 293 
PRO   N   CA   sing N N 294 
PRO   N   CD   sing N N 295 
PRO   N   H    sing N N 296 
PRO   CA  C    sing N N 297 
PRO   CA  CB   sing N N 298 
PRO   CA  HA   sing N N 299 
PRO   C   O    doub N N 300 
PRO   C   OXT  sing N N 301 
PRO   CB  CG   sing N N 302 
PRO   CB  HB2  sing N N 303 
PRO   CB  HB3  sing N N 304 
PRO   CG  CD   sing N N 305 
PRO   CG  HG2  sing N N 306 
PRO   CG  HG3  sing N N 307 
PRO   CD  HD2  sing N N 308 
PRO   CD  HD3  sing N N 309 
PRO   OXT HXT  sing N N 310 
SER   N   CA   sing N N 311 
SER   N   H    sing N N 312 
SER   N   H2   sing N N 313 
SER   CA  C    sing N N 314 
SER   CA  CB   sing N N 315 
SER   CA  HA   sing N N 316 
SER   C   O    doub N N 317 
SER   C   OXT  sing N N 318 
SER   CB  OG   sing N N 319 
SER   CB  HB2  sing N N 320 
SER   CB  HB3  sing N N 321 
SER   OG  HG   sing N N 322 
SER   OXT HXT  sing N N 323 
TFA   C1  C2   sing N N 324 
TFA   C1  O    doub N N 325 
TFA   C1  OXT  sing N N 326 
TFA   C2  F1   sing N N 327 
TFA   C2  F2   sing N N 328 
TFA   C2  F3   sing N N 329 
TFA   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TYR   N   CA   sing N N 347 
TYR   N   H    sing N N 348 
TYR   N   H2   sing N N 349 
TYR   CA  C    sing N N 350 
TYR   CA  CB   sing N N 351 
TYR   CA  HA   sing N N 352 
TYR   C   O    doub N N 353 
TYR   C   OXT  sing N N 354 
TYR   CB  CG   sing N N 355 
TYR   CB  HB2  sing N N 356 
TYR   CB  HB3  sing N N 357 
TYR   CG  CD1  doub Y N 358 
TYR   CG  CD2  sing Y N 359 
TYR   CD1 CE1  sing Y N 360 
TYR   CD1 HD1  sing N N 361 
TYR   CD2 CE2  doub Y N 362 
TYR   CD2 HD2  sing N N 363 
TYR   CE1 CZ   doub Y N 364 
TYR   CE1 HE1  sing N N 365 
TYR   CE2 CZ   sing Y N 366 
TYR   CE2 HE2  sing N N 367 
TYR   CZ  OH   sing N N 368 
TYR   OH  HH   sing N N 369 
TYR   OXT HXT  sing N N 370 
VAL   N   CA   sing N N 371 
VAL   N   H    sing N N 372 
VAL   N   H2   sing N N 373 
VAL   CA  C    sing N N 374 
VAL   CA  CB   sing N N 375 
VAL   CA  HA   sing N N 376 
VAL   C   O    doub N N 377 
VAL   C   OXT  sing N N 378 
VAL   CB  CG1  sing N N 379 
VAL   CB  CG2  sing N N 380 
VAL   CB  HB   sing N N 381 
VAL   CG1 HG11 sing N N 382 
VAL   CG1 HG12 sing N N 383 
VAL   CG1 HG13 sing N N 384 
VAL   CG2 HG21 sing N N 385 
VAL   CG2 HG22 sing N N 386 
VAL   CG2 HG23 sing N N 387 
VAL   OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HD0 
_atom_sites.fract_transf_matrix[1][1]   0.011261 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011261 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025331 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . VAL   A 1 3   ? 19.587 -16.158 22.273  1.00 55.16 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.640 -15.066 22.457  1.00 54.67 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.300 -13.733 22.122  1.00 52.31 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.422 -13.463 22.551  1.00 52.99 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.061 -15.061 23.887  1.00 56.08 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 17.053 -13.932 24.054  1.00 56.43 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.420 -16.405 24.206  1.00 56.46 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.899 -15.188 21.847  1.00 65.59 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.780 -14.916 24.522  1.00 67.28 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.578 -14.054 24.891  1.00 67.70 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.523 -13.084 24.062  1.00 67.70 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.426 -13.958 23.314  1.00 67.70 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.995 -16.354 25.076  1.00 67.73 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.759 -16.607 23.526  1.00 67.73 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.107 -17.090 24.213  1.00 67.73 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.603 -12.904 21.345  1.00 48.67 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.055 -11.556 21.023  1.00 44.57 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.924 -10.567 21.298  1.00 40.21 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.817 -10.949 21.692  1.00 40.21 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.601 -11.456 19.591  1.00 44.26 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.585 -11.854 18.544  1.00 43.70 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.470 -11.335 18.513  1.00 43.52 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.969 -12.783 17.673  1.00 43.56 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.846 -13.109 20.990  1.00 58.38 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.782 -11.333 21.616  1.00 53.47 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.868 -10.538 19.419  1.00 53.09 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.367 -12.044 19.506  1.00 53.09 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.432 -13.044 17.055  1.00 52.25 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.758 -13.125 17.728  1.00 52.25 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.198 -9.283  21.069  0.70 37.75 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.223 -9.284  21.100  0.30 37.98 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.285 -8.211  21.447  0.70 35.17 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.316 -8.200  21.452  0.30 35.57 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.414 -7.718  20.294  0.70 31.88 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.450 -7.736  20.288  0.30 32.50 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.756 -6.683  20.434  0.70 32.15 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.663 -6.800  20.458  0.30 32.62 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.062 -7.040  22.053  0.70 36.01 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.101 -7.014  22.026  0.30 36.20 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 19.034 -6.550  21.147  0.70 36.43 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 19.010 -6.490  21.075  0.30 36.50 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.917 -9.008  20.687  0.70 45.28 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.962 -9.015  20.752  0.30 45.56 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.693 -8.546  22.137  0.70 42.19 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.717 -8.511  22.142  0.30 42.67 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.441 -6.324  22.263  0.70 43.20 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.476 -6.317  22.283  0.30 43.43 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.504 -7.340  22.864  0.70 43.20 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.597 -7.313  22.806  0.30 43.43 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.456 -5.911  21.497  0.70 43.70 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.431 -5.842  21.408  0.30 43.78 ?  5   SER   A HG   1 
ATOM   52   N  N    A PHE   A 1 6   ? 16.387 -8.425  19.167  0.70 27.84 ?  6   PHE   A N    1 
ATOM   53   N  N    B PHE   A 1 6   ? 16.571 -8.359  19.118  0.30 29.09 ?  6   PHE   A N    1 
ATOM   54   C  CA   A PHE   A 1 6   ? 15.487 -8.049  18.084  0.70 23.88 ?  6   PHE   A CA   1 
ATOM   55   C  CA   B PHE   A 1 6   ? 15.669 -8.057  18.015  0.30 25.70 ?  6   PHE   A CA   1 
ATOM   56   C  C    A PHE   A 1 6   ? 14.052 -8.413  18.453  0.70 23.32 ?  6   PHE   A C    1 
ATOM   57   C  C    B PHE   A 1 6   ? 14.250 -8.443  18.406  0.30 24.54 ?  6   PHE   A C    1 
ATOM   58   O  O    A PHE   A 1 6   ? 13.795 -9.475  19.023  0.70 24.37 ?  6   PHE   A O    1 
ATOM   59   O  O    B PHE   A 1 6   ? 13.947 -9.627  18.579  0.30 24.39 ?  6   PHE   A O    1 
ATOM   60   C  CB   A PHE   A 1 6   ? 15.890 -8.753  16.792  0.70 21.40 ?  6   PHE   A CB   1 
ATOM   61   C  CB   B PHE   A 1 6   ? 16.092 -8.818  16.761  0.30 23.84 ?  6   PHE   A CB   1 
ATOM   62   C  CG   A PHE   A 1 6   ? 17.177 -8.237  16.197  0.70 19.40 ?  6   PHE   A CG   1 
ATOM   63   C  CG   B PHE   A 1 6   ? 17.359 -8.304  16.136  0.30 22.22 ?  6   PHE   A CG   1 
ATOM   64   C  CD1  A PHE   A 1 6   ? 17.195 -7.060  15.468  0.70 18.49 ?  6   PHE   A CD1  1 
ATOM   65   C  CD1  B PHE   A 1 6   ? 17.381 -7.077  15.495  0.30 21.49 ?  6   PHE   A CD1  1 
ATOM   66   C  CD2  A PHE   A 1 6   ? 18.360 -8.935  16.363  0.70 19.67 ?  6   PHE   A CD2  1 
ATOM   67   C  CD2  B PHE   A 1 6   ? 18.522 -9.054  16.176  0.30 21.76 ?  6   PHE   A CD2  1 
ATOM   68   C  CE1  A PHE   A 1 6   ? 18.373 -6.585  14.918  0.70 18.46 ?  6   PHE   A CE1  1 
ATOM   69   C  CE1  B PHE   A 1 6   ? 18.542 -6.603  14.914  0.30 21.26 ?  6   PHE   A CE1  1 
ATOM   70   C  CE2  A PHE   A 1 6   ? 19.537 -8.469  15.815  0.70 19.63 ?  6   PHE   A CE2  1 
ATOM   71   C  CE2  B PHE   A 1 6   ? 19.686 -8.586  15.595  0.30 21.44 ?  6   PHE   A CE2  1 
ATOM   72   C  CZ   A PHE   A 1 6   ? 19.543 -7.292  15.091  0.70 18.94 ?  6   PHE   A CZ   1 
ATOM   73   C  CZ   B PHE   A 1 6   ? 19.696 -7.359  14.963  0.30 21.25 ?  6   PHE   A CZ   1 
ATOM   74   H  H    A PHE   A 1 6   ? 16.867 -9.121  19.010  0.70 33.40 ?  6   PHE   A H    1 
ATOM   75   H  H    B PHE   A 1 6   ? 17.162 -8.959  18.936  0.30 34.90 ?  6   PHE   A H    1 
ATOM   76   H  HA   A PHE   A 1 6   ? 15.529 -7.096  17.947  0.70 28.64 ?  6   PHE   A HA   1 
ATOM   77   H  HA   B PHE   A 1 6   ? 15.685 -7.104  17.828  0.30 30.82 ?  6   PHE   A HA   1 
ATOM   78   H  HB2  A PHE   A 1 6   ? 16.004 -9.701  16.974  0.70 25.66 ?  6   PHE   A HB2  1 
ATOM   79   H  HB2  B PHE   A 1 6   ? 16.233 -9.748  17.001  0.30 28.59 ?  6   PHE   A HB2  1 
ATOM   80   H  HB3  A PHE   A 1 6   ? 15.186 -8.629  16.136  0.70 25.66 ?  6   PHE   A HB3  1 
ATOM   81   H  HB3  B PHE   A 1 6   ? 15.385 -8.750  16.104  0.30 28.59 ?  6   PHE   A HB3  1 
ATOM   82   H  HD1  A PHE   A 1 6   ? 16.401 -6.585  15.349  0.70 22.17 ?  6   PHE   A HD1  1 
ATOM   83   H  HD1  B PHE   A 1 6   ? 16.606 -6.564  15.462  0.30 25.78 ?  6   PHE   A HD1  1 
ATOM   84   H  HD2  A PHE   A 1 6   ? 18.360 -9.729  16.853  0.70 23.59 ?  6   PHE   A HD2  1 
ATOM   85   H  HD2  B PHE   A 1 6   ? 18.521 -9.882  16.603  0.30 26.10 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  A PHE   A 1 6   ? 18.370 -5.795  14.430  0.70 22.13 ?  6   PHE   A HE1  1 
ATOM   87   H  HE1  B PHE   A 1 6   ? 18.545 -5.776  14.488  0.30 25.49 ?  6   PHE   A HE1  1 
ATOM   88   H  HE2  A PHE   A 1 6   ? 20.328 -8.943  15.936  0.70 23.54 ?  6   PHE   A HE2  1 
ATOM   89   H  HE2  B PHE   A 1 6   ? 20.463 -9.097  15.630  0.30 25.72 ?  6   PHE   A HE2  1 
ATOM   90   H  HZ   A PHE   A 1 6   ? 20.334 -6.973  14.723  0.70 22.71 ?  6   PHE   A HZ   1 
ATOM   91   H  HZ   B PHE   A 1 6   ? 20.478 -7.042  14.572  0.30 25.48 ?  6   PHE   A HZ   1 
ATOM   92   N  N    A SER   A 1 7   ? 13.111 -7.525  18.124  0.70 21.61 ?  7   SER   A N    1 
ATOM   93   N  N    B SER   A 1 7   ? 13.373 -7.452  18.538  0.30 23.63 ?  7   SER   A N    1 
ATOM   94   C  CA   A SER   A 1 7   ? 11.735 -7.637  18.598  0.70 21.42 ?  7   SER   A CA   1 
ATOM   95   C  CA   B SER   A 1 7   ? 12.035 -7.651  19.074  0.30 23.18 ?  7   SER   A CA   1 
ATOM   96   C  C    A SER   A 1 7   ? 10.739 -7.407  17.467  0.70 19.02 ?  7   SER   A C    1 
ATOM   97   C  C    B SER   A 1 7   ? 10.996 -7.351  18.005  0.30 21.56 ?  7   SER   A C    1 
ATOM   98   O  O    A SER   A 1 7   ? 10.935 -6.528  16.623  0.70 19.03 ?  7   SER   A O    1 
ATOM   99   O  O    B SER   A 1 7   ? 11.159 -6.421  17.208  0.30 21.49 ?  7   SER   A O    1 
ATOM   100  C  CB   A SER   A 1 7   ? 11.479 -6.612  19.713  0.70 23.56 ?  7   SER   A CB   1 
ATOM   101  C  CB   B SER   A 1 7   ? 11.803 -6.742  20.284  0.30 24.14 ?  7   SER   A CB   1 
ATOM   102  O  OG   A SER   A 1 7   ? 10.131 -6.644  20.144  0.70 25.23 ?  7   SER   A OG   1 
ATOM   103  O  OG   B SER   A 1 7   ? 10.545 -6.996  20.882  0.30 24.81 ?  7   SER   A OG   1 
ATOM   104  H  H    A SER   A 1 7   ? 13.248 -6.845  17.617  0.70 25.91 ?  7   SER   A H    1 
ATOM   105  H  H    B SER   A 1 7   ? 13.536 -6.640  18.308  0.30 28.34 ?  7   SER   A H    1 
ATOM   106  H  HA   A SER   A 1 7   ? 11.588 -8.525  18.960  0.70 25.69 ?  7   SER   A HA   1 
ATOM   107  H  HA   B SER   A 1 7   ? 11.928 -8.571  19.356  0.30 27.81 ?  7   SER   A HA   1 
ATOM   108  H  HB2  A SER   A 1 7   ? 12.060 -6.816  20.465  0.70 28.26 ?  7   SER   A HB2  1 
ATOM   109  H  HB2  B SER   A 1 7   ? 12.501 -6.907  20.938  0.30 28.95 ?  7   SER   A HB2  1 
ATOM   110  H  HB3  A SER   A 1 7   ? 11.678 -5.725  19.376  0.70 28.26 ?  7   SER   A HB3  1 
ATOM   111  H  HB3  B SER   A 1 7   ? 11.834 -5.817  19.994  0.30 28.95 ?  7   SER   A HB3  1 
ATOM   112  H  HG   A SER   A 1 7   ? 10.014 -6.083  20.760  0.70 30.26 ?  7   SER   A HG   1 
ATOM   113  H  HG   B SER   A 1 7   ? 10.434 -6.490  21.543  0.30 29.76 ?  7   SER   A HG   1 
ATOM   114  N  N    A GLY   A 1 8   ? 9.660  -8.193  17.468  0.70 17.57 ?  8   GLY   A N    1 
ATOM   115  N  N    B GLY   A 1 8   ? 9.933  -8.152  17.988  0.30 20.04 ?  8   GLY   A N    1 
ATOM   116  C  CA   A GLY   A 1 8   ? 8.567  -7.975  16.539  0.70 16.71 ?  8   GLY   A CA   1 
ATOM   117  C  CA   B GLY   A 1 8   ? 8.816  -7.915  17.099  0.30 18.55 ?  8   GLY   A CA   1 
ATOM   118  C  C    A GLY   A 1 8   ? 8.790  -8.469  15.129  0.70 15.28 ?  8   GLY   A C    1 
ATOM   119  C  C    B GLY   A 1 8   ? 8.982  -8.422  15.687  0.30 16.97 ?  8   GLY   A C    1 
ATOM   120  O  O    A GLY   A 1 8   ? 8.068  -8.047  14.219  0.70 15.62 ?  8   GLY   A O    1 
ATOM   121  O  O    B GLY   A 1 8   ? 8.145  -8.101  14.836  0.30 16.80 ?  8   GLY   A O    1 
ATOM   122  H  H    A GLY   A 1 8   ? 9.542  -8.857  18.004  0.70 21.07 ?  8   GLY   A H    1 
ATOM   123  H  H    B GLY   A 1 8   ? 9.838  -8.845  18.489  0.30 24.04 ?  8   GLY   A H    1 
ATOM   124  H  HA2  A GLY   A 1 8   ? 7.772  -8.410  16.891  0.70 20.04 ?  8   GLY   A HA2  1 
ATOM   125  H  HA2  B GLY   A 1 8   ? 8.027  -8.338  17.464  0.30 22.24 ?  8   GLY   A HA2  1 
ATOM   126  H  HA3  A GLY   A 1 8   ? 8.386  -7.023  16.493  0.70 20.04 ?  8   GLY   A HA3  1 
ATOM   127  H  HA3  B GLY   A 1 8   ? 8.653  -6.962  17.048  0.30 22.24 ?  8   GLY   A HA3  1 
ATOM   128  N  N    A TYR   A 1 9   ? 9.766  -9.349  14.911  0.70 14.05 ?  9   TYR   A N    1 
ATOM   129  N  N    B TYR   A 1 9   ? 10.021 -9.202  15.405  0.30 15.95 ?  9   TYR   A N    1 
ATOM   130  C  CA   A TYR   A 1 9   ? 10.043 -9.883  13.586  0.70 13.16 ?  9   TYR   A CA   1 
ATOM   131  C  CA   B TYR   A 1 9   ? 10.228 -9.702  14.056  0.30 15.00 ?  9   TYR   A CA   1 
ATOM   132  C  C    A TYR   A 1 9   ? 9.197  -11.119 13.312  0.70 12.52 ?  9   TYR   A C    1 
ATOM   133  C  C    B TYR   A 1 9   ? 9.342  -10.909 13.780  0.30 14.26 ?  9   TYR   A C    1 
ATOM   134  O  O    A TYR   A 1 9   ? 8.958  -11.943 14.200  0.70 14.01 ?  9   TYR   A O    1 
ATOM   135  O  O    B TYR   A 1 9   ? 9.049  -11.713 14.671  0.30 15.09 ?  9   TYR   A O    1 
ATOM   136  C  CB   A TYR   A 1 9   ? 11.523 -10.255 13.443  0.70 13.60 ?  9   TYR   A CB   1 
ATOM   137  C  CB   B TYR   A 1 9   ? 11.696 -10.077 13.836  0.30 15.16 ?  9   TYR   A CB   1 
ATOM   138  C  CG   A TYR   A 1 9   ? 12.436 -9.062  13.292  0.70 14.21 ?  9   TYR   A CG   1 
ATOM   139  C  CG   B TYR   A 1 9   ? 12.580 -8.875  13.600  0.30 15.10 ?  9   TYR   A CG   1 
ATOM   140  C  CD1  A TYR   A 1 9   ? 12.776 -8.287  14.391  0.70 14.77 ?  9   TYR   A CD1  1 
ATOM   141  C  CD1  B TYR   A 1 9   ? 12.905 -8.018  14.641  0.30 15.41 ?  9   TYR   A CD1  1 
ATOM   142  C  CD2  A TYR   A 1 9   ? 12.940 -8.700  12.050  0.70 13.98 ?  9   TYR   A CD2  1 
ATOM   143  C  CD2  B TYR   A 1 9   ? 13.073 -8.586  12.334  0.30 14.74 ?  9   TYR   A CD2  1 
ATOM   144  C  CE1  A TYR   A 1 9   ? 13.593 -7.186  14.261  0.70 15.76 ?  9   TYR   A CE1  1 
ATOM   145  C  CE1  B TYR   A 1 9   ? 13.702 -6.910  14.432  0.30 15.66 ?  9   TYR   A CE1  1 
ATOM   146  C  CE2  A TYR   A 1 9   ? 13.755 -7.601  11.908  0.70 14.52 ?  9   TYR   A CE2  1 
ATOM   147  C  CE2  B TYR   A 1 9   ? 13.870 -7.479  12.115  0.30 15.14 ?  9   TYR   A CE2  1 
ATOM   148  C  CZ   A TYR   A 1 9   ? 14.071 -6.847  13.015  0.70 15.68 ?  9   TYR   A CZ   1 
ATOM   149  C  CZ   B TYR   A 1 9   ? 14.179 -6.645  13.168  0.30 15.80 ?  9   TYR   A CZ   1 
ATOM   150  O  OH   A TYR   A 1 9   ? 14.878 -5.751  12.865  0.70 17.09 ?  9   TYR   A OH   1 
ATOM   151  O  OH   B TYR   A 1 9   ? 14.969 -5.541  12.957  0.30 16.66 ?  9   TYR   A OH   1 
ATOM   152  H  H    A TYR   A 1 9   ? 10.277 -9.661  15.524  0.70 16.85 ?  9   TYR   A H    1 
ATOM   153  H  H    B TYR   A 1 9   ? 10.620 -9.455  15.973  0.30 19.13 ?  9   TYR   A H    1 
ATOM   154  H  HA   A TYR   A 1 9   ? 9.828  -9.215  12.916  0.70 15.78 ?  9   TYR   A HA   1 
ATOM   155  H  HA   B TYR   A 1 9   ? 10.004 -9.005  13.420  0.30 17.98 ?  9   TYR   A HA   1 
ATOM   156  H  HB2  A TYR   A 1 9   ? 11.800 -10.750 14.229  0.70 16.31 ?  9   TYR   A HB2  1 
ATOM   157  H  HB2  B TYR   A 1 9   ? 12.030 -10.551 14.614  0.30 18.17 ?  9   TYR   A HB2  1 
ATOM   158  H  HB3  A TYR   A 1 9   ? 11.620 -10.807 12.652  0.70 16.31 ?  9   TYR   A HB3  1 
ATOM   159  H  HB3  B TYR   A 1 9   ? 11.756 -10.648 13.053  0.30 18.17 ?  9   TYR   A HB3  1 
ATOM   160  H  HD1  A TYR   A 1 9   ? 12.438 -8.514  15.231  0.70 17.71 ?  9   TYR   A HD1  1 
ATOM   161  H  HD1  B TYR   A 1 9   ? 12.581 -8.195  15.495  0.30 18.48 ?  9   TYR   A HD1  1 
ATOM   162  H  HD2  A TYR   A 1 9   ? 12.717 -9.208  11.301  0.70 16.77 ?  9   TYR   A HD2  1 
ATOM   163  H  HD2  B TYR   A 1 9   ? 12.866 -9.148  11.621  0.30 17.67 ?  9   TYR   A HD2  1 
ATOM   164  H  HE1  A TYR   A 1 9   ? 13.815 -6.675  15.005  0.70 18.90 ?  9   TYR   A HE1  1 
ATOM   165  H  HE1  B TYR   A 1 9   ? 13.911 -6.345  15.139  0.30 18.77 ?  9   TYR   A HE1  1 
ATOM   166  H  HE2  A TYR   A 1 9   ? 14.092 -7.370  11.070  0.70 17.41 ?  9   TYR   A HE2  1 
ATOM   167  H  HE2  B TYR   A 1 9   ? 14.197 -7.296  11.262  0.30 18.15 ?  9   TYR   A HE2  1 
ATOM   168  H  HH   A TYR   A 1 9   ? 15.024 -5.391  13.611  0.70 20.50 ?  9   TYR   A HH   1 
ATOM   169  H  HH   B TYR   A 1 9   ? 15.077 -5.123  13.677  0.30 19.97 ?  9   TYR   A HH   1 
ATOM   170  N  N    A LEU   A 1 10  ? 8.756  -11.244 12.066  0.70 12.25 ?  10  LEU   A N    1 
ATOM   171  N  N    B LEU   A 1 10  ? 8.909  -11.022 12.527  0.30 13.60 ?  10  LEU   A N    1 
ATOM   172  C  CA   A LEU   A 1 10  ? 8.178  -12.486 11.576  0.70 11.65 ?  10  LEU   A CA   1 
ATOM   173  C  CA   B LEU   A 1 10  ? 8.207  -12.201 12.045  0.30 13.53 ?  10  LEU   A CA   1 
ATOM   174  C  C    A LEU   A 1 10  ? 9.306  -13.425 11.147  0.70 11.87 ?  10  LEU   A C    1 
ATOM   175  C  C    B LEU   A 1 10  ? 9.245  -13.183 11.518  0.30 12.77 ?  10  LEU   A C    1 
ATOM   176  O  O    A LEU   A 1 10  ? 10.269 -13.005 10.500  0.70 12.51 ?  10  LEU   A O    1 
ATOM   177  O  O    B LEU   A 1 10  ? 10.113 -12.810 10.724  0.30 12.79 ?  10  LEU   A O    1 
ATOM   178  C  CB   A LEU   A 1 10  ? 7.284  -12.171 10.380  0.70 12.42 ?  10  LEU   A CB   1 
ATOM   179  C  CB   B LEU   A 1 10  ? 7.238  -11.815 10.928  0.30 13.81 ?  10  LEU   A CB   1 
ATOM   180  C  CG   A LEU   A 1 10  ? 6.592  -13.348 9.702   0.70 15.02 ?  10  LEU   A CG   1 
ATOM   181  C  CG   B LEU   A 1 10  ? 6.453  -12.958 10.291  0.30 14.57 ?  10  LEU   A CG   1 
ATOM   182  C  CD1  A LEU   A 1 10  ? 5.562  -13.954 10.627  0.70 16.40 ?  10  LEU   A CD1  1 
ATOM   183  C  CD1  B LEU   A 1 10  ? 5.496  -13.554 11.304  0.30 15.37 ?  10  LEU   A CD1  1 
ATOM   184  C  CD2  A LEU   A 1 10  ? 5.959  -12.921 8.387   0.70 16.30 ?  10  LEU   A CD2  1 
ATOM   185  C  CD2  B LEU   A 1 10  ? 5.708  -12.440 9.080   0.30 15.53 ?  10  LEU   A CD2  1 
ATOM   186  H  H    A LEU   A 1 10  ? 8.779  -10.616 11.473  0.70 14.68 ?  10  LEU   A H    1 
ATOM   187  H  H    B LEU   A 1 10  ? 9.021  -10.416 11.923  0.30 16.30 ?  10  LEU   A H    1 
ATOM   188  H  HA   A LEU   A 1 10  ? 7.646  -12.909 12.273  0.70 13.97 ?  10  LEU   A HA   1 
ATOM   189  H  HA   B LEU   A 1 10  ? 7.708  -12.614 12.767  0.30 16.22 ?  10  LEU   A HA   1 
ATOM   190  H  HB2  A LEU   A 1 10  ? 6.584  -11.569 10.670  0.70 14.89 ?  10  LEU   A HB2  1 
ATOM   191  H  HB2  B LEU   A 1 10  ? 6.584  -11.188 11.286  0.30 16.55 ?  10  LEU   A HB2  1 
ATOM   192  H  HB3  A LEU   A 1 10  ? 7.824  -11.739 9.704   0.70 14.89 ?  10  LEU   A HB3  1 
ATOM   193  H  HB3  B LEU   A 1 10  ? 7.739  -11.381 10.220  0.30 16.55 ?  10  LEU   A HB3  1 
ATOM   194  H  HG   A LEU   A 1 10  ? 7.250  -14.037 9.503   0.70 18.01 ?  10  LEU   A HG   1 
ATOM   195  H  HG   B LEU   A 1 10  ? 7.067  -13.652 10.000  0.30 17.46 ?  10  LEU   A HG   1 
ATOM   196  H  HD11 A LEU   A 1 10  ? 5.176  -14.740 10.207  0.70 19.67 ?  10  LEU   A HD11 1 
ATOM   197  H  HD11 B LEU   A 1 10  ? 5.028  -14.298 10.895  0.30 18.42 ?  10  LEU   A HD11 1 
ATOM   198  H  HD12 A LEU   A 1 10  ? 5.989  -14.204 11.461  0.70 19.67 ?  10  LEU   A HD12 1 
ATOM   199  H  HD12 B LEU   A 1 10  ? 5.997  -13.862 12.074  0.30 18.42 ?  10  LEU   A HD12 1 
ATOM   200  H  HD13 A LEU   A 1 10  ? 4.867  -13.297 10.798  0.70 19.67 ?  10  LEU   A HD13 1 
ATOM   201  H  HD13 B LEU   A 1 10  ? 4.861  -12.872 11.574  0.30 18.42 ?  10  LEU   A HD13 1 
ATOM   202  H  HD21 A LEU   A 1 10  ? 5.526  -13.690 7.981   0.70 19.55 ?  10  LEU   A HD21 1 
ATOM   203  H  HD21 B LEU   A 1 10  ? 5.208  -13.169 8.683   0.30 18.62 ?  10  LEU   A HD21 1 
ATOM   204  H  HD22 A LEU   A 1 10  ? 5.305  -12.229 8.567   0.70 19.55 ?  10  LEU   A HD22 1 
ATOM   205  H  HD22 B LEU   A 1 10  ? 5.103  -11.737 9.363   0.30 18.62 ?  10  LEU   A HD22 1 
ATOM   206  H  HD23 A LEU   A 1 10  ? 6.652  -12.582 7.801   0.70 19.55 ?  10  LEU   A HD23 1 
ATOM   207  H  HD23 B LEU   A 1 10  ? 6.349  -12.089 8.443   0.30 18.62 ?  10  LEU   A HD23 1 
ATOM   208  N  N    A LYS   A 1 11  ? 9.190  -14.701 11.513  0.70 12.32 ?  11  LYS   A N    1 
ATOM   209  N  N    B LYS   A 1 11  ? 9.168  -14.427 11.976  0.30 12.46 ?  11  LYS   A N    1 
ATOM   210  C  CA   A LYS   A 1 11  ? 10.203 -15.699 11.188  0.70 12.51 ?  11  LYS   A CA   1 
ATOM   211  C  CA   B LYS   A 1 11  ? 10.116 -15.449 11.555  0.30 12.31 ?  11  LYS   A CA   1 
ATOM   212  C  C    A LYS   A 1 11  ? 9.866  -16.301 9.832   0.70 12.52 ?  11  LYS   A C    1 
ATOM   213  C  C    B LYS   A 1 11  ? 9.716  -15.966 10.179  0.30 11.49 ?  11  LYS   A C    1 
ATOM   214  O  O    A LYS   A 1 11  ? 8.799  -16.897 9.670   0.70 14.20 ?  11  LYS   A O    1 
ATOM   215  O  O    B LYS   A 1 11  ? 8.585  -16.424 9.986   0.30 11.38 ?  11  LYS   A O    1 
ATOM   216  C  CB   A LYS   A 1 11  ? 10.243 -16.771 12.278  0.70 12.68 ?  11  LYS   A CB   1 
ATOM   217  C  CB   B LYS   A 1 11  ? 10.147 -16.581 12.579  0.30 12.78 ?  11  LYS   A CB   1 
ATOM   218  C  CG   A LYS   A 1 11  ? 11.268 -17.885 12.092  0.70 13.16 ?  11  LYS   A CG   1 
ATOM   219  C  CG   B LYS   A 1 11  ? 11.159 -17.680 12.283  0.30 13.02 ?  11  LYS   A CG   1 
ATOM   220  C  CD   A LYS   A 1 11  ? 11.377 -18.701 13.383  0.70 13.82 ?  11  LYS   A CD   1 
ATOM   221  C  CD   B LYS   A 1 11  ? 11.187 -18.719 13.398  0.30 13.40 ?  11  LYS   A CD   1 
ATOM   222  C  CE   A LYS   A 1 11  ? 12.359 -19.860 13.283  0.70 14.30 ?  11  LYS   A CE   1 
ATOM   223  C  CE   B LYS   A 1 11  ? 12.210 -19.817 13.134  0.30 13.59 ?  11  LYS   A CE   1 
ATOM   224  N  NZ   A LYS   A 1 11  ? 13.741 -19.410 12.964  0.70 14.64 ?  11  LYS   A NZ   1 
ATOM   225  N  NZ   B LYS   A 1 11  ? 13.605 -19.294 13.082  0.30 13.56 ?  11  LYS   A NZ   1 
ATOM   226  H  H    A LYS   A 1 11  ? 8.514  -15.023 11.938  0.70 14.77 ?  11  LYS   A H    1 
ATOM   227  H  H    B LYS   A 1 11  ? 8.576  -14.700 12.533  0.30 14.94 ?  11  LYS   A H    1 
ATOM   228  H  HA   A LYS   A 1 11  ? 11.073 -15.274 11.131  0.70 14.99 ?  11  LYS   A HA   1 
ATOM   229  H  HA   B LYS   A 1 11  ? 11.001 -15.058 11.491  0.30 14.76 ?  11  LYS   A HA   1 
ATOM   230  H  HB2  A LYS   A 1 11  ? 10.444 -16.333 13.120  0.70 15.19 ?  11  LYS   A HB2  1 
ATOM   231  H  HB2  B LYS   A 1 11  ? 10.368 -16.201 13.444  0.30 15.32 ?  11  LYS   A HB2  1 
ATOM   232  H  HB3  A LYS   A 1 11  ? 9.372  -17.186 12.329  0.70 15.19 ?  11  LYS   A HB3  1 
ATOM   233  H  HB3  B LYS   A 1 11  ? 9.270  -16.986 12.614  0.30 15.32 ?  11  LYS   A HB3  1 
ATOM   234  H  HG2  A LYS   A 1 11  ? 10.986 -18.473 11.374  0.70 15.77 ?  11  LYS   A HG2  1 
ATOM   235  H  HG2  B LYS   A 1 11  ? 10.916 -18.126 11.457  0.30 15.61 ?  11  LYS   A HG2  1 
ATOM   236  H  HG3  A LYS   A 1 11  ? 12.139 -17.501 11.896  0.70 15.77 ?  11  LYS   A HG3  1 
ATOM   237  H  HG3  B LYS   A 1 11  ? 12.044 -17.290 12.207  0.30 15.61 ?  11  LYS   A HG3  1 
ATOM   238  H  HD2  A LYS   A 1 11  ? 11.670 -18.121 14.100  0.70 16.57 ?  11  LYS   A HD2  1 
ATOM   239  H  HD2  B LYS   A 1 11  ? 11.420 -18.284 14.233  0.30 16.06 ?  11  LYS   A HD2  1 
ATOM   240  H  HD3  A LYS   A 1 11  ? 10.503 -19.071 13.592  0.70 16.57 ?  11  LYS   A HD3  1 
ATOM   241  H  HD3  B LYS   A 1 11  ? 10.312 -19.132 13.469  0.30 16.06 ?  11  LYS   A HD3  1 
ATOM   242  H  HE2  A LYS   A 1 11  ? 12.386 -20.329 14.132  0.70 17.14 ?  11  LYS   A HE2  1 
ATOM   243  H  HE2  B LYS   A 1 11  ? 12.164 -20.475 13.846  0.30 16.29 ?  11  LYS   A HE2  1 
ATOM   244  H  HE3  A LYS   A 1 11  ? 12.072 -20.464 12.580  0.70 17.14 ?  11  LYS   A HE3  1 
ATOM   245  H  HE3  B LYS   A 1 11  ? 12.016 -20.238 12.281  0.30 16.29 ?  11  LYS   A HE3  1 
ATOM   246  H  HZ1  A LYS   A 1 11  ? 14.277 -20.115 12.866  0.70 17.56 ?  11  LYS   A HZ1  1 
ATOM   247  H  HZ1  B LYS   A 1 11  ? 14.177 -19.962 12.941  0.30 16.26 ?  11  LYS   A HZ1  1 
ATOM   248  H  HZ2  A LYS   A 1 11  ? 13.742 -18.941 12.208  0.70 17.56 ?  11  LYS   A HZ2  1 
ATOM   249  H  HZ2  B LYS   A 1 11  ? 13.684 -18.703 12.421  0.30 16.26 ?  11  LYS   A HZ2  1 
ATOM   250  H  HZ3  A LYS   A 1 11  ? 14.055 -18.899 13.621  0.70 17.56 ?  11  LYS   A HZ3  1 
ATOM   251  H  HZ3  B LYS   A 1 11  ? 13.810 -18.897 13.852  0.30 16.26 ?  11  LYS   A HZ3  1 
ATOM   252  N  N    A LEU   A 1 12  ? 10.766 -16.156 8.858   0.70 12.16 ?  12  LEU   A N    1 
ATOM   253  N  N    B LEU   A 1 12  ? 10.631 -15.866 9.215   0.30 11.62 ?  12  LEU   A N    1 
ATOM   254  C  CA   A LEU   A 1 12  ? 10.512 -16.739 7.544   0.70 11.95 ?  12  LEU   A CA   1 
ATOM   255  C  CA   B LEU   A 1 12  ? 10.395 -16.363 7.864   0.30 11.95 ?  12  LEU   A CA   1 
ATOM   256  C  C    A LEU   A 1 12  ? 11.107 -18.135 7.400   0.70 11.84 ?  12  LEU   A C    1 
ATOM   257  C  C    B LEU   A 1 12  ? 10.959 -17.762 7.652   0.30 12.17 ?  12  LEU   A C    1 
ATOM   258  O  O    A LEU   A 1 12  ? 10.479 -19.010 6.792   0.70 12.00 ?  12  LEU   A O    1 
ATOM   259  O  O    B LEU   A 1 12  ? 10.282 -18.627 7.086   0.30 12.10 ?  12  LEU   A O    1 
ATOM   260  C  CB   A LEU   A 1 12  ? 11.052 -15.841 6.426   0.70 11.99 ?  12  LEU   A CB   1 
ATOM   261  C  CB   B LEU   A 1 12  ? 10.985 -15.399 6.824   0.30 12.86 ?  12  LEU   A CB   1 
ATOM   262  C  CG   A LEU   A 1 12  ? 10.398 -14.472 6.244   0.70 12.99 ?  12  LEU   A CG   1 
ATOM   263  C  CG   B LEU   A 1 12  ? 10.267 -14.055 6.685   0.30 13.69 ?  12  LEU   A CG   1 
ATOM   264  C  CD1  A LEU   A 1 12  ? 11.153 -13.686 5.195   0.70 13.02 ?  12  LEU   A CD1  1 
ATOM   265  C  CD1  B LEU   A 1 12  ? 10.763 -13.294 5.462   0.30 14.03 ?  12  LEU   A CD1  1 
ATOM   266  C  CD2  A LEU   A 1 12  ? 8.922  -14.613 5.864   0.70 13.77 ?  12  LEU   A CD2  1 
ATOM   267  C  CD2  B LEU   A 1 12  ? 8.766  -14.270 6.607   0.30 14.06 ?  12  LEU   A CD2  1 
ATOM   268  H  H    A LEU   A 1 12  ? 11.523 -15.731 8.927   0.70 14.57 ?  12  LEU   A H    1 
ATOM   269  H  H    B LEU   A 1 12  ? 11.405 -15.495 9.319   0.30 13.93 ?  12  LEU   A H    1 
ATOM   270  H  HA   A LEU   A 1 12  ? 9.558  -16.819 7.426   0.70 14.32 ?  12  LEU   A HA   1 
ATOM   271  H  HA   B LEU   A 1 12  ? 9.442  -16.419 7.720   0.30 14.32 ?  12  LEU   A HA   1 
ATOM   272  H  HB2  A LEU   A 1 12  ? 11.992 -15.688 6.589   0.70 14.38 ?  12  LEU   A HB2  1 
ATOM   273  H  HB2  B LEU   A 1 12  ? 11.907 -15.211 7.063   0.30 15.42 ?  12  LEU   A HB2  1 
ATOM   274  H  HB3  A LEU   A 1 12  ? 10.947 -16.320 5.586   0.70 14.38 ?  12  LEU   A HB3  1 
ATOM   275  H  HB3  B LEU   A 1 12  ? 10.960 -15.831 5.955   0.30 15.42 ?  12  LEU   A HB3  1 
ATOM   276  H  HG   A LEU   A 1 12  ? 10.445 -13.985 7.080   0.70 15.57 ?  12  LEU   A HG   1 
ATOM   277  H  HG   B LEU   A 1 12  ? 10.451 -13.512 7.468   0.30 16.41 ?  12  LEU   A HG   1 
ATOM   278  H  HD11 A LEU   A 1 12  ? 10.733 -12.822 5.082   0.70 15.61 ?  12  LEU   A HD11 1 
ATOM   279  H  HD11 B LEU   A 1 12  ? 10.296 -12.443 5.408   0.30 16.83 ?  12  LEU   A HD11 1 
ATOM   280  H  HD12 A LEU   A 1 12  ? 12.072 -13.574 5.490   0.70 15.61 ?  12  LEU   A HD12 1 
ATOM   281  H  HD12 B LEU   A 1 12  ? 11.716 -13.144 5.548   0.30 16.83 ?  12  LEU   A HD12 1 
ATOM   282  H  HD13 A LEU   A 1 12  ? 11.135 -14.178 4.358   0.70 15.61 ?  12  LEU   A HD13 1 
ATOM   283  H  HD13 B LEU   A 1 12  ? 10.579 -13.820 4.668   0.30 16.83 ?  12  LEU   A HD13 1 
ATOM   284  H  HD21 A LEU   A 1 12  ? 8.552  -13.734 5.688   0.70 16.51 ?  12  LEU   A HD21 1 
ATOM   285  H  HD21 B LEU   A 1 12  ? 8.351  -13.481 6.233   0.30 16.85 ?  12  LEU   A HD21 1 
ATOM   286  H  HD22 A LEU   A 1 12  ? 8.849  -15.166 5.068   0.70 16.51 ?  12  LEU   A HD22 1 
ATOM   287  H  HD22 B LEU   A 1 12  ? 8.589  -15.040 6.043   0.30 16.85 ?  12  LEU   A HD22 1 
ATOM   288  H  HD23 A LEU   A 1 12  ? 8.440  -15.031 6.597   0.70 16.51 ?  12  LEU   A HD23 1 
ATOM   289  H  HD23 B LEU   A 1 12  ? 8.425  -14.432 7.502   0.30 16.85 ?  12  LEU   A HD23 1 
ATOM   290  N  N    A THR   A 1 13  ? 12.312 -18.344 7.923   0.70 12.16 ?  13  THR   A N    1 
ATOM   291  N  N    B THR   A 1 13  ? 12.195 -17.991 8.080   0.30 12.35 ?  13  THR   A N    1 
ATOM   292  C  CA   A THR   A 1 13  ? 13.014 -19.619 7.842   0.70 12.41 ?  13  THR   A CA   1 
ATOM   293  C  CA   B THR   A 1 13  ? 12.833 -19.292 7.967   0.30 12.23 ?  13  THR   A CA   1 
ATOM   294  C  C    A THR   A 1 13  ? 13.785 -19.823 9.140   0.70 12.80 ?  13  THR   A C    1 
ATOM   295  C  C    B THR   A 1 13  ? 13.587 -19.565 9.260   0.30 12.67 ?  13  THR   A C    1 
ATOM   296  O  O    A THR   A 1 13  ? 13.691 -19.027 10.078  0.70 12.94 ?  13  THR   A O    1 
ATOM   297  O  O    B THR   A 1 13  ? 13.465 -18.837 10.251  0.30 13.11 ?  13  THR   A O    1 
ATOM   298  C  CB   A THR   A 1 13  ? 13.996 -19.666 6.661   0.70 13.35 ?  13  THR   A CB   1 
ATOM   299  C  CB   B THR   A 1 13  ? 13.781 -19.344 6.761   0.30 12.28 ?  13  THR   A CB   1 
ATOM   300  O  OG1  A THR   A 1 13  ? 15.070 -18.751 6.905   0.70 13.66 ?  13  THR   A OG1  1 
ATOM   301  O  OG1  B THR   A 1 13  ? 14.832 -18.390 6.947   0.30 12.20 ?  13  THR   A OG1  1 
ATOM   302  C  CG2  A THR   A 1 13  ? 13.325 -19.317 5.345   0.70 14.12 ?  13  THR   A CG2  1 
ATOM   303  C  CG2  B THR   A 1 13  ? 13.042 -19.050 5.454   0.30 12.60 ?  13  THR   A CG2  1 
ATOM   304  H  H    A THR   A 1 13  ? 12.764 -17.740 8.334   0.70 14.57 ?  13  THR   A H    1 
ATOM   305  H  H    B THR   A 1 13  ? 12.693 -17.388 8.436   0.30 14.81 ?  13  THR   A H    1 
ATOM   306  H  HA   A THR   A 1 13  ? 12.374 -20.344 7.739   0.70 14.87 ?  13  THR   A HA   1 
ATOM   307  H  HA   B THR   A 1 13  ? 12.157 -19.975 7.857   0.30 14.67 ?  13  THR   A HA   1 
ATOM   308  H  HB   A THR   A 1 13  ? 14.358 -20.565 6.581   0.70 16.00 ?  13  THR   A HB   1 
ATOM   309  H  HB   B THR   A 1 13  ? 14.167 -20.232 6.694   0.30 14.72 ?  13  THR   A HB   1 
ATOM   310  H  HG1  A THR   A 1 13  ? 15.613 -18.768 6.258   0.70 16.38 ?  13  THR   A HG1  1 
ATOM   311  H  HG1  B THR   A 1 13  ? 15.357 -18.408 6.289   0.30 14.62 ?  13  THR   A HG1  1 
ATOM   312  H  HG21 A THR   A 1 13  ? 13.941 -19.474 4.610   0.70 16.93 ?  13  THR   A HG21 1 
ATOM   313  H  HG21 B THR   A 1 13  ? 13.650 -19.142 4.701   0.30 15.10 ?  13  THR   A HG21 1 
ATOM   314  H  HG22 A THR   A 1 13  ? 12.539 -19.872 5.217   0.70 16.93 ?  13  THR   A HG22 1 
ATOM   315  H  HG22 B THR   A 1 13  ? 12.309 -19.678 5.340   0.30 15.10 ?  13  THR   A HG22 1 
ATOM   316  H  HG23 A THR   A 1 13  ? 13.061 -18.387 5.344   0.70 16.93 ?  13  THR   A HG23 1 
ATOM   317  H  HG23 B THR   A 1 13  ? 12.687 -18.150 5.465   0.30 15.10 ?  13  THR   A HG23 1 
ATOM   318  N  N    A ASP   A 1 14  ? 14.599 -20.880 9.173   0.70 13.40 ?  14  ASP   A N    1 
ATOM   319  N  N    B ASP   A 1 14  ? 14.388 -20.627 9.228   0.30 13.26 ?  14  ASP   A N    1 
ATOM   320  C  CA   A ASP   A 1 14  ? 15.439 -21.125 10.337  0.70 14.74 ?  14  ASP   A CA   1 
ATOM   321  C  CA   B ASP   A 1 14  ? 15.234 -20.968 10.361  0.30 14.15 ?  14  ASP   A CA   1 
ATOM   322  C  C    A ASP   A 1 14  ? 16.253 -19.900 10.734  0.70 14.35 ?  14  ASP   A C    1 
ATOM   323  C  C    B ASP   A 1 14  ? 16.131 -19.800 10.750  0.30 13.71 ?  14  ASP   A C    1 
ATOM   324  O  O    A ASP   A 1 14  ? 16.512 -19.689 11.924  0.70 15.38 ?  14  ASP   A O    1 
ATOM   325  O  O    B ASP   A 1 14  ? 16.321 -19.526 11.941  0.30 14.06 ?  14  ASP   A O    1 
ATOM   326  C  CB   A ASP   A 1 14  ? 16.392 -22.284 10.057  0.70 17.75 ?  14  ASP   A CB   1 
ATOM   327  C  CB   B ASP   A 1 14  ? 16.067 -22.195 10.002  0.30 15.85 ?  14  ASP   A CB   1 
ATOM   328  C  CG   A ASP   A 1 14  ? 17.309 -22.564 11.226  0.70 21.82 ?  14  ASP   A CG   1 
ATOM   329  C  CG   B ASP   A 1 14  ? 17.019 -22.587 11.100  0.30 17.70 ?  14  ASP   A CG   1 
ATOM   330  O  OD1  A ASP   A 1 14  ? 16.815 -23.043 12.268  0.70 23.65 ?  14  ASP   A OD1  1 
ATOM   331  O  OD1  B ASP   A 1 14  ? 16.539 -22.947 12.197  0.30 18.46 ?  14  ASP   A OD1  1 
ATOM   332  O  OD2  A ASP   A 1 14  ? 18.519 -22.277 11.110  0.70 24.26 -1 14  ASP   A OD2  1 
ATOM   333  O  OD2  B ASP   A 1 14  ? 18.242 -22.539 10.865  0.30 18.95 -1 14  ASP   A OD2  1 
ATOM   334  H  H    A ASP   A 1 14  ? 14.693 -21.459 8.537   0.70 16.07 ?  14  ASP   A H    1 
ATOM   335  H  H    B ASP   A 1 14  ? 14.465 -21.153 8.561   0.30 15.90 ?  14  ASP   A H    1 
ATOM   336  H  HA   A ASP   A 1 14  ? 14.878 -21.374 11.087  0.70 17.67 ?  14  ASP   A HA   1 
ATOM   337  H  HA   B ASP   A 1 14  ? 14.682 -21.188 11.125  0.30 16.96 ?  14  ASP   A HA   1 
ATOM   338  H  HB2  A ASP   A 1 14  ? 15.870 -23.091 9.875   0.70 21.28 ?  14  ASP   A HB2  1 
ATOM   339  H  HB2  B ASP   A 1 14  ? 15.472 -22.948 9.849   0.30 19.01 ?  14  ASP   A HB2  1 
ATOM   340  H  HB3  A ASP   A 1 14  ? 16.941 -22.073 9.286   0.70 21.28 ?  14  ASP   A HB3  1 
ATOM   341  H  HB3  B ASP   A 1 14  ? 16.576 -22.012 9.193   0.30 19.01 ?  14  ASP   A HB3  1 
ATOM   342  N  N    . ASN   A 1 15  ? 16.674 -19.085 9.763   1.00 13.48 ?  15  ASN   A N    1 
ATOM   343  C  CA   . ASN   A 1 15  ? 17.657 -18.041 10.024  1.00 14.09 ?  15  ASN   A CA   1 
ATOM   344  C  C    . ASN   A 1 15  ? 17.287 -16.652 9.527   1.00 14.16 ?  15  ASN   A C    1 
ATOM   345  O  O    . ASN   A 1 15  ? 18.074 -15.728 9.748   1.00 15.70 ?  15  ASN   A O    1 
ATOM   346  C  CB   . ASN   A 1 15  ? 19.032 -18.439 9.448   1.00 13.74 ?  15  ASN   A CB   1 
ATOM   347  C  CG   . ASN   A 1 15  ? 19.023 -18.536 7.940   1.00 14.21 ?  15  ASN   A CG   1 
ATOM   348  O  OD1  . ASN   A 1 15  ? 18.308 -19.358 7.362   1.00 15.22 ?  15  ASN   A OD1  1 
ATOM   349  N  ND2  . ASN   A 1 15  ? 19.815 -17.687 7.286   1.00 14.24 ?  15  ASN   A ND2  1 
ATOM   350  H  H    A ASN   A 1 15  ? 16.403 -19.116 8.951   0.70 16.16 ?  15  ASN   A H    1 
ATOM   351  H  H    B ASN   A 1 15  ? 16.480 -19.182 8.934   0.30 16.16 ?  15  ASN   A H    1 
ATOM   352  H  HA   . ASN   A 1 15  ? 17.779 -17.966 10.982  1.00 16.89 ?  15  ASN   A HA   1 
ATOM   353  H  HB2  . ASN   A 1 15  ? 19.691 -17.765 9.706   1.00 16.48 ?  15  ASN   A HB2  1 
ATOM   354  H  HB3  . ASN   A 1 15  ? 19.294 -19.302 9.806   1.00 16.48 ?  15  ASN   A HB3  1 
ATOM   355  H  HD21 . ASN   A 1 15  ? 19.840 -17.700 6.426   1.00 17.07 ?  15  ASN   A HD21 1 
ATOM   356  H  HD22 . ASN   A 1 15  ? 20.299 -17.117 7.717   1.00 17.07 ?  15  ASN   A HD22 1 
ATOM   357  N  N    A VAL   A 1 16  ? 16.176 -16.492 8.810   0.70 13.55 ?  16  VAL   A N    1 
ATOM   358  N  N    B VAL   A 1 16  ? 16.098 -16.440 8.965   0.30 13.48 ?  16  VAL   A N    1 
ATOM   359  C  CA   A VAL   A 1 16  ? 15.784 -15.218 8.219   0.70 13.34 ?  16  VAL   A CA   1 
ATOM   360  C  CA   B VAL   A 1 16  ? 15.716 -15.144 8.412   0.30 12.76 ?  16  VAL   A CA   1 
ATOM   361  C  C    A VAL   A 1 16  ? 14.496 -14.731 8.869   0.70 12.59 ?  16  VAL   A C    1 
ATOM   362  C  C    B VAL   A 1 16  ? 14.475 -14.621 9.133   0.30 12.47 ?  16  VAL   A C    1 
ATOM   363  O  O    A VAL   A 1 16  ? 13.484 -15.447 8.909   0.70 12.01 ?  16  VAL   A O    1 
ATOM   364  O  O    B VAL   A 1 16  ? 13.511 -15.363 9.357   0.30 12.33 ?  16  VAL   A O    1 
ATOM   365  C  CB   A VAL   A 1 16  ? 15.636 -15.304 6.691   0.70 14.03 ?  16  VAL   A CB   1 
ATOM   366  C  CB   B VAL   A 1 16  ? 15.498 -15.225 6.886   0.30 12.70 ?  16  VAL   A CB   1 
ATOM   367  C  CG1  A VAL   A 1 16  ? 15.216 -13.947 6.125   0.70 14.99 ?  16  VAL   A CG1  1 
ATOM   368  C  CG1  B VAL   A 1 16  ? 15.086 -13.872 6.317   0.30 13.23 ?  16  VAL   A CG1  1 
ATOM   369  C  CG2  A VAL   A 1 16  ? 16.931 -15.770 6.048   0.70 14.71 ?  16  VAL   A CG2  1 
ATOM   370  C  CG2  B VAL   A 1 16  ? 16.761 -15.739 6.193   0.30 13.23 ?  16  VAL   A CG2  1 
ATOM   371  H  H    A VAL   A 1 16  ? 15.626 -17.136 8.648   0.70 16.25 ?  16  VAL   A H    1 
ATOM   372  H  H    B VAL   A 1 16  ? 15.483 -17.038 8.905   0.30 16.16 ?  16  VAL   A H    1 
ATOM   373  H  HA   A VAL   A 1 16  ? 16.480 -14.571 8.406   0.70 15.99 ?  16  VAL   A HA   1 
ATOM   374  H  HA   B VAL   A 1 16  ? 16.434 -14.510 8.565   0.30 15.30 ?  16  VAL   A HA   1 
ATOM   375  H  HB   A VAL   A 1 16  ? 14.946 -15.950 6.474   0.70 16.82 ?  16  VAL   A HB   1 
ATOM   376  H  HB   B VAL   A 1 16  ? 14.787 -15.855 6.704   0.30 15.22 ?  16  VAL   A HB   1 
ATOM   377  H  HG11 A VAL   A 1 16  ? 15.324 -13.962 5.162   0.70 17.98 ?  16  VAL   A HG11 1 
ATOM   378  H  HG11 B VAL   A 1 16  ? 15.132 -13.913 5.347   0.30 15.86 ?  16  VAL   A HG11 1 
ATOM   379  H  HG12 A VAL   A 1 16  ? 14.287 -13.785 6.351   0.70 17.98 ?  16  VAL   A HG12 1 
ATOM   380  H  HG12 B VAL   A 1 16  ? 14.178 -13.676 6.594   0.30 15.86 ?  16  VAL   A HG12 1 
ATOM   381  H  HG13 A VAL   A 1 16  ? 15.779 -13.259 6.511   0.70 17.98 ?  16  VAL   A HG13 1 
ATOM   382  H  HG13 B VAL   A 1 16  ? 15.692 -13.191 6.646   0.30 15.86 ?  16  VAL   A HG13 1 
ATOM   383  H  HG21 A VAL   A 1 16  ? 16.840 -15.723 5.084   0.70 17.64 ?  16  VAL   A HG21 1 
ATOM   384  H  HG21 B VAL   A 1 16  ? 16.628 -15.714 5.232   0.30 15.86 ?  16  VAL   A HG21 1 
ATOM   385  H  HG22 A VAL   A 1 16  ? 17.654 -15.196 6.341   0.70 17.64 ?  16  VAL   A HG22 1 
ATOM   386  H  HG22 B VAL   A 1 16  ? 17.511 -15.174 6.436   0.30 15.86 ?  16  VAL   A HG22 1 
ATOM   387  H  HG23 A VAL   A 1 16  ? 17.106 -16.686 6.319   0.70 17.64 ?  16  VAL   A HG23 1 
ATOM   388  H  HG23 B VAL   A 1 16  ? 16.931 -16.651 6.479   0.30 15.86 ?  16  VAL   A HG23 1 
ATOM   389  N  N    A TYR   A 1 17  ? 14.539 -13.486 9.330   0.70 12.53 ?  17  TYR   A N    1 
ATOM   390  N  N    B TYR   A 1 17  ? 14.508 -13.330 9.486   0.30 12.41 ?  17  TYR   A N    1 
ATOM   391  C  CA   A TYR   A 1 17  ? 13.451 -12.797 10.001  0.70 12.37 ?  17  TYR   A CA   1 
ATOM   392  C  CA   B TYR   A 1 17  ? 13.450 -12.660 10.233  0.30 11.99 ?  17  TYR   A CA   1 
ATOM   393  C  C    A TYR   A 1 17  ? 13.175 -11.489 9.266   0.70 12.35 ?  17  TYR   A C    1 
ATOM   394  C  C    B TYR   A 1 17  ? 13.193 -11.297 9.600   0.30 11.58 ?  17  TYR   A C    1 
ATOM   395  O  O    A TYR   A 1 17  ? 14.067 -10.939 8.618   0.70 12.23 ?  17  TYR   A O    1 
ATOM   396  O  O    B TYR   A 1 17  ? 14.111 -10.683 9.053   0.30 11.12 ?  17  TYR   A O    1 
ATOM   397  C  CB   A TYR   A 1 17  ? 13.874 -12.506 11.443  0.70 13.13 ?  17  TYR   A CB   1 
ATOM   398  C  CB   B TYR   A 1 17  ? 13.869 -12.467 11.698  0.30 12.53 ?  17  TYR   A CB   1 
ATOM   399  C  CG   A TYR   A 1 17  ? 14.042 -13.757 12.275  0.70 14.65 ?  17  TYR   A CG   1 
ATOM   400  C  CG   B TYR   A 1 17  ? 14.146 -13.757 12.446  0.30 13.08 ?  17  TYR   A CG   1 
ATOM   401  C  CD1  A TYR   A 1 17  ? 15.203 -14.527 12.208  0.70 15.69 ?  17  TYR   A CD1  1 
ATOM   402  C  CD1  B TYR   A 1 17  ? 15.348 -14.439 12.285  0.30 13.48 ?  17  TYR   A CD1  1 
ATOM   403  C  CD2  A TYR   A 1 17  ? 13.023 -14.184 13.115  0.70 14.81 ?  17  TYR   A CD2  1 
ATOM   404  C  CD2  B TYR   A 1 17  ? 13.207 -14.286 13.320  0.30 13.29 ?  17  TYR   A CD2  1 
ATOM   405  C  CE1  A TYR   A 1 17  ? 15.338 -15.689 12.963  0.70 15.95 ?  17  TYR   A CE1  1 
ATOM   406  C  CE1  B TYR   A 1 17  ? 15.600 -15.619 12.967  0.30 13.98 ?  17  TYR   A CE1  1 
ATOM   407  C  CE2  A TYR   A 1 17  ? 13.149 -15.339 13.871  0.70 15.35 ?  17  TYR   A CE2  1 
ATOM   408  C  CE2  B TYR   A 1 17  ? 13.450 -15.466 14.009  0.30 13.72 ?  17  TYR   A CE2  1 
ATOM   409  C  CZ   A TYR   A 1 17  ? 14.306 -16.088 13.796  0.70 15.55 ?  17  TYR   A CZ   1 
ATOM   410  C  CZ   B TYR   A 1 17  ? 14.648 -16.129 13.829  0.30 13.98 ?  17  TYR   A CZ   1 
ATOM   411  O  OH   A TYR   A 1 17  ? 14.416 -17.236 14.555  0.70 16.09 ?  17  TYR   A OH   1 
ATOM   412  O  OH   B TYR   A 1 17  ? 14.895 -17.301 14.513  0.30 14.43 ?  17  TYR   A OH   1 
ATOM   413  H  H    A TYR   A 1 17  ? 15.244 -13.005 9.258   0.70 15.02 ?  17  TYR   A H    1 
ATOM   414  H  H    B TYR   A 1 17  ? 15.164 -12.797 9.297   0.30 14.87 ?  17  TYR   A H    1 
ATOM   415  H  HA   A TYR   A 1 17  ? 12.657 -13.360 9.999   0.70 14.82 ?  17  TYR   A HA   1 
ATOM   416  H  HA   B TYR   A 1 17  ? 12.631 -13.174 10.198  0.30 14.37 ?  17  TYR   A HA   1 
ATOM   417  H  HB2  A TYR   A 1 17  ? 14.719 -12.039 11.434  0.70 15.74 ?  17  TYR   A HB2  1 
ATOM   418  H  HB2  B TYR   A 1 17  ? 14.677 -11.933 11.718  0.30 15.02 ?  17  TYR   A HB2  1 
ATOM   419  H  HB3  A TYR   A 1 17  ? 13.193 -11.963 11.859  0.70 15.74 ?  17  TYR   A HB3  1 
ATOM   420  H  HB3  B TYR   A 1 17  ? 13.158 -12.002 12.165  0.30 15.02 ?  17  TYR   A HB3  1 
ATOM   421  H  HD1  A TYR   A 1 17  ? 15.899 -14.266 11.647  0.70 18.81 ?  17  TYR   A HD1  1 
ATOM   422  H  HD1  B TYR   A 1 17  ? 15.989 -14.102 11.702  0.30 16.16 ?  17  TYR   A HD1  1 
ATOM   423  H  HD2  A TYR   A 1 17  ? 12.238 -13.692 13.173  0.70 17.75 ?  17  TYR   A HD2  1 
ATOM   424  H  HD2  B TYR   A 1 17  ? 12.397 -13.841 13.441  0.30 15.93 ?  17  TYR   A HD2  1 
ATOM   425  H  HE1  A TYR   A 1 17  ? 16.123 -16.197 12.914  0.70 19.13 ?  17  TYR   A HE1  1 
ATOM   426  H  HE1  B TYR   A 1 17  ? 16.408 -16.064 12.849  0.30 16.76 ?  17  TYR   A HE1  1 
ATOM   427  H  HE2  A TYR   A 1 17  ? 12.458 -15.609 14.433  0.70 18.40 ?  17  TYR   A HE2  1 
ATOM   428  H  HE2  B TYR   A 1 17  ? 12.809 -15.803 14.591  0.30 16.45 ?  17  TYR   A HE2  1 
ATOM   429  H  HH   A TYR   A 1 17  ? 13.659 -17.468 14.833  0.70 19.30 ?  17  TYR   A HH   1 
ATOM   430  H  HH   B TYR   A 1 17  ? 15.632 -17.622 14.272  0.30 17.30 ?  17  TYR   A HH   1 
ATOM   431  N  N    A ILE   A 1 18  ? 11.945 -10.972 9.368   0.70 12.43 ?  18  ILE   A N    1 
ATOM   432  N  N    B ILE   A 1 18  ? 11.948 -10.809 9.683   0.30 11.39 ?  18  ILE   A N    1 
ATOM   433  C  CA   A ILE   A 1 18  ? 11.553 -9.792  8.594   0.70 12.12 ?  18  ILE   A CA   1 
ATOM   434  C  CA   B ILE   A 1 18  ? 11.555 -9.589  8.979   0.30 10.63 ?  18  ILE   A CA   1 
ATOM   435  C  C    A ILE   A 1 18  ? 10.575 -8.926  9.383   0.70 12.45 ?  18  ILE   A C    1 
ATOM   436  C  C    B ILE   A 1 18  ? 10.641 -8.727  9.843   0.30 10.54 ?  18  ILE   A C    1 
ATOM   437  O  O    A ILE   A 1 18  ? 9.744  -9.430  10.141  0.70 12.60 ?  18  ILE   A O    1 
ATOM   438  O  O    B ILE   A 1 18  ? 9.823  -9.232  10.619  0.30 11.05 ?  18  ILE   A O    1 
ATOM   439  C  CB   A ILE   A 1 18  ? 11.011 -10.210 7.205   0.70 11.84 ?  18  ILE   A CB   1 
ATOM   440  C  CB   B ILE   A 1 18  ? 10.897 -9.914  7.618   0.30 10.26 ?  18  ILE   A CB   1 
ATOM   441  C  CG1  A ILE   A 1 18  ? 10.966 -9.018  6.257   0.70 12.31 ?  18  ILE   A CG1  1 
ATOM   442  C  CG1  B ILE   A 1 18  ? 10.809 -8.670  6.730   0.30 11.21 ?  18  ILE   A CG1  1 
ATOM   443  C  CG2  A ILE   A 1 18  ? 9.660  -10.925 7.330   0.70 11.85 ?  18  ILE   A CG2  1 
ATOM   444  C  CG2  B ILE   A 1 18  ? 9.521  -10.536 7.817   0.30 10.60 ?  18  ILE   A CG2  1 
ATOM   445  C  CD1  A ILE   A 1 18  ? 10.731 -9.413  4.830   0.70 13.59 ?  18  ILE   A CD1  1 
ATOM   446  C  CD1  B ILE   A 1 18  ? 10.389 -8.991  5.309   0.30 12.46 ?  18  ILE   A CD1  1 
ATOM   447  H  H    A ILE   A 1 18  ? 11.332 -11.299 9.876   0.70 14.90 ?  18  ILE   A H    1 
ATOM   448  H  H    B ILE   A 1 18  ? 11.312 -11.169 10.137  0.30 13.65 ?  18  ILE   A H    1 
ATOM   449  H  HA   A ILE   A 1 18  ? 12.350 -9.269  8.439   0.70 14.53 ?  18  ILE   A HA   1 
ATOM   450  H  HA   B ILE   A 1 18  ? 12.356 -9.069  8.799   0.30 12.74 ?  18  ILE   A HA   1 
ATOM   451  H  HB   A ILE   A 1 18  ? 11.637 -10.855 6.829   0.70 14.19 ?  18  ILE   A HB   1 
ATOM   452  H  HB   B ILE   A 1 18  ? 11.457 -10.558 7.170   0.30 12.29 ?  18  ILE   A HB   1 
ATOM   453  H  HG12 A ILE   A 1 18  ? 10.252 -8.427  6.529   0.70 14.76 ?  18  ILE   A HG12 1 
ATOM   454  H  HG12 B ILE   A 1 18  ? 10.157 -8.054  7.101   0.30 13.44 ?  18  ILE   A HG12 1 
ATOM   455  H  HG13 A ILE   A 1 18  ? 11.819 -8.554  6.298   0.70 14.76 ?  18  ILE   A HG13 1 
ATOM   456  H  HG13 B ILE   A 1 18  ? 11.681 -8.242  6.692   0.30 13.44 ?  18  ILE   A HG13 1 
ATOM   457  H  HG21 A ILE   A 1 18  ? 9.425  -11.311 6.467   0.70 14.20 ?  18  ILE   A HG21 1 
ATOM   458  H  HG21 B ILE   A 1 18  ? 9.227  -10.917 6.974   0.30 12.70 ?  18  ILE   A HG21 1 
ATOM   459  H  HG22 A ILE   A 1 18  ? 9.734  -11.632 7.991   0.70 14.20 ?  18  ILE   A HG22 1 
ATOM   460  H  HG22 B ILE   A 1 18  ? 9.584  -11.228 8.490   0.30 12.70 ?  18  ILE   A HG22 1 
ATOM   461  H  HG23 A ILE   A 1 18  ? 8.986  -10.287 7.599   0.70 14.20 ?  18  ILE   A HG23 1 
ATOM   462  H  HG23 B ILE   A 1 18  ? 8.898  -9.849  8.103   0.30 12.70 ?  18  ILE   A HG23 1 
ATOM   463  H  HD11 A ILE   A 1 18  ? 10.776 -8.617  4.274   0.70 16.29 ?  18  ILE   A HD11 1 
ATOM   464  H  HD11 B ILE   A 1 18  ? 10.457 -8.192  4.766   0.30 14.94 ?  18  ILE   A HD11 1 
ATOM   465  H  HD12 A ILE   A 1 18  ? 11.408 -10.047 4.558   0.70 16.29 ?  18  ILE   A HD12 1 
ATOM   466  H  HD12 B ILE   A 1 18  ? 10.975 -9.680  4.956   0.30 14.94 ?  18  ILE   A HD12 1 
ATOM   467  H  HD13 A ILE   A 1 18  ? 9.849  -9.813  4.757   0.70 16.29 ?  18  ILE   A HD13 1 
ATOM   468  H  HD13 B ILE   A 1 18  ? 9.473  -9.310  5.315   0.30 14.94 ?  18  ILE   A HD13 1 
ATOM   469  N  N    A LYS   A 1 19  ? 10.664 -7.607  9.179   0.70 12.36 ?  19  LYS   A N    1 
ATOM   470  N  N    B LYS   A 1 19  ? 10.777 -7.408  9.683   0.30 10.58 ?  19  LYS   A N    1 
ATOM   471  C  CA   A LYS   A 1 19  ? 9.843  -6.641  9.903   0.70 12.64 ?  19  LYS   A CA   1 
ATOM   472  C  CA   B LYS   A 1 19  ? 10.012 -6.445  10.462  0.30 11.86 ?  19  LYS   A CA   1 
ATOM   473  C  C    A LYS   A 1 19  ? 9.675  -5.385  9.057   0.70 12.15 ?  19  LYS   A C    1 
ATOM   474  C  C    B LYS   A 1 19  ? 9.790  -5.207  9.612   0.30 12.27 ?  19  LYS   A C    1 
ATOM   475  O  O    A LYS   A 1 19  ? 10.574 -5.012  8.302   0.70 12.16 ?  19  LYS   A O    1 
ATOM   476  O  O    B LYS   A 1 19  ? 10.681 -4.798  8.865   0.30 11.97 ?  19  LYS   A O    1 
ATOM   477  C  CB   A LYS   A 1 19  ? 10.535 -6.272  11.222  0.70 14.04 ?  19  LYS   A CB   1 
ATOM   478  C  CB   B LYS   A 1 19  ? 10.783 -6.066  11.732  0.30 12.54 ?  19  LYS   A CB   1 
ATOM   479  C  CG   A LYS   A 1 19  ? 9.784  -5.313  12.132  0.70 15.64 ?  19  LYS   A CG   1 
ATOM   480  C  CG   B LYS   A 1 19  ? 10.062 -5.161  12.709  0.30 13.62 ?  19  LYS   A CG   1 
ATOM   481  C  CD   A LYS   A 1 19  ? 10.627 -5.023  13.369  0.70 17.51 ?  19  LYS   A CD   1 
ATOM   482  C  CD   B LYS   A 1 19  ? 10.981 -4.878  13.886  0.30 14.60 ?  19  LYS   A CD   1 
ATOM   483  C  CE   A LYS   A 1 19  ? 9.948  -4.076  14.341  0.70 18.80 ?  19  LYS   A CE   1 
ATOM   484  C  CE   B LYS   A 1 19  ? 10.329 -4.027  14.951  0.30 14.90 ?  19  LYS   A CE   1 
ATOM   485  N  NZ   A LYS   A 1 19  ? 10.839 -3.767  15.497  0.70 19.26 ?  19  LYS   A NZ   1 
ATOM   486  N  NZ   B LYS   A 1 19  ? 11.255 -3.867  16.108  0.30 14.83 ?  19  LYS   A NZ   1 
ATOM   487  H  H    A LYS   A 1 19  ? 11.210 -7.253  8.620   0.70 14.81 ?  19  LYS   A H    1 
ATOM   488  H  H    B LYS   A 1 19  ? 11.321 -7.031  9.117   0.30 12.68 ?  19  LYS   A H    1 
ATOM   489  H  HA   A LYS   A 1 19  ? 8.970  -7.035  10.096  0.70 15.15 ?  19  LYS   A HA   1 
ATOM   490  H  HA   B LYS   A 1 19  ? 9.155  -6.813  10.709  0.30 14.22 ?  19  LYS   A HA   1 
ATOM   491  H  HB2  A LYS   A 1 19  ? 10.684 -7.089  11.726  0.70 16.83 ?  19  LYS   A HB2  1 
ATOM   492  H  HB2  B LYS   A 1 19  ? 10.994 -6.880  12.213  0.30 15.03 ?  19  LYS   A HB2  1 
ATOM   493  H  HB3  A LYS   A 1 19  ? 11.386 -5.867  11.008  0.70 16.83 ?  19  LYS   A HB3  1 
ATOM   494  H  HB3  B LYS   A 1 19  ? 11.605 -5.616  11.479  0.30 15.03 ?  19  LYS   A HB3  1 
ATOM   495  H  HG2  A LYS   A 1 19  ? 9.623  -4.478  11.665  0.70 18.76 ?  19  LYS   A HG2  1 
ATOM   496  H  HG2  B LYS   A 1 19  ? 9.841  -4.320  12.280  0.30 16.33 ?  19  LYS   A HG2  1 
ATOM   497  H  HG3  A LYS   A 1 19  ? 8.947  -5.715  12.414  0.70 18.76 ?  19  LYS   A HG3  1 
ATOM   498  H  HG3  B LYS   A 1 19  ? 9.262  -5.601  13.038  0.30 16.33 ?  19  LYS   A HG3  1 
ATOM   499  H  HD2  A LYS   A 1 19  ? 10.802 -5.856  13.837  0.70 20.99 ?  19  LYS   A HD2  1 
ATOM   500  H  HD2  B LYS   A 1 19  ? 11.233 -5.722  14.293  0.30 17.50 ?  19  LYS   A HD2  1 
ATOM   501  H  HD3  A LYS   A 1 19  ? 11.466 -4.618  13.094  0.70 20.99 ?  19  LYS   A HD3  1 
ATOM   502  H  HD3  B LYS   A 1 19  ? 11.770 -4.414  13.567  0.30 17.50 ?  19  LYS   A HD3  1 
ATOM   503  H  HE2  A LYS   A 1 19  ? 9.739  -3.245  13.888  0.70 22.55 ?  19  LYS   A HE2  1 
ATOM   504  H  HE2  B LYS   A 1 19  ? 10.131 -3.150  14.588  0.30 17.86 ?  19  LYS   A HE2  1 
ATOM   505  H  HE3  A LYS   A 1 19  ? 9.140  -4.489  14.682  0.70 22.55 ?  19  LYS   A HE3  1 
ATOM   506  H  HE3  B LYS   A 1 19  ? 9.518  -4.460  15.261  0.30 17.86 ?  19  LYS   A HE3  1 
ATOM   507  H  HZ1  A LYS   A 1 19  ? 10.416 -3.243  16.077  0.70 23.09 ?  19  LYS   A HZ1  1 
ATOM   508  H  HZ1  B LYS   A 1 19  ? 10.870 -3.369  16.736  0.30 17.78 ?  19  LYS   A HZ1  1 
ATOM   509  H  HZ2  A LYS   A 1 19  ? 11.076 -4.521  15.908  0.70 23.09 ?  19  LYS   A HZ2  1 
ATOM   510  H  HZ2  B LYS   A 1 19  ? 11.453 -4.664  16.450  0.30 17.78 ?  19  LYS   A HZ2  1 
ATOM   511  H  HZ3  A LYS   A 1 19  ? 11.573 -3.352  15.213  0.70 23.09 ?  19  LYS   A HZ3  1 
ATOM   512  H  HZ3  B LYS   A 1 19  ? 12.005 -3.470  15.843  0.30 17.78 ?  19  LYS   A HZ3  1 
ATOM   513  N  N    A ASN   A 1 20  ? 8.512  -4.738  9.181   0.70 13.08 ?  20  ASN   A N    1 
ATOM   514  N  N    B ASN   A 1 20  ? 8.600  -4.620  9.716   0.30 13.23 ?  20  ASN   A N    1 
ATOM   515  C  CA   A ASN   A 1 20  ? 8.296  -3.415  8.587   0.70 14.31 ?  20  ASN   A CA   1 
ATOM   516  C  CA   B ASN   A 1 20  ? 8.348  -3.310  9.122   0.30 14.21 ?  20  ASN   A CA   1 
ATOM   517  C  C    A ASN   A 1 20  ? 8.891  -2.384  9.539   0.70 15.81 ?  20  ASN   A C    1 
ATOM   518  C  C    B ASN   A 1 20  ? 9.022  -2.287  10.020  0.30 14.86 ?  20  ASN   A C    1 
ATOM   519  O  O    A ASN   A 1 20  ? 8.321  -2.098  10.595  0.70 17.55 ?  20  ASN   A O    1 
ATOM   520  O  O    B ASN   A 1 20  ? 8.556  -2.004  11.126  0.30 15.19 ?  20  ASN   A O    1 
ATOM   521  C  CB   A ASN   A 1 20  ? 6.805  -3.179  8.352   0.70 14.95 ?  20  ASN   A CB   1 
ATOM   522  C  CB   B ASN   A 1 20  ? 6.852  -3.043  8.997   0.30 14.82 ?  20  ASN   A CB   1 
ATOM   523  C  CG   A ASN   A 1 20  ? 6.483  -1.751  7.916   0.70 16.22 ?  20  ASN   A CG   1 
ATOM   524  C  CG   B ASN   A 1 20  ? 6.537  -1.574  8.750   0.30 15.70 ?  20  ASN   A CG   1 
ATOM   525  O  OD1  A ASN   A 1 20  ? 5.493  -1.163  8.361   0.70 18.46 ?  20  ASN   A OD1  1 
ATOM   526  O  OD1  B ASN   A 1 20  ? 5.711  -0.981  9.441   0.30 16.61 ?  20  ASN   A OD1  1 
ATOM   527  N  ND2  A ASN   A 1 20  ? 7.315  -1.193  7.040   0.70 16.79 ?  20  ASN   A ND2  1 
ATOM   528  N  ND2  B ASN   A 1 20  ? 7.208  -0.980  7.770   0.30 15.58 ?  20  ASN   A ND2  1 
ATOM   529  H  H    A ASN   A 1 20  ? 7.827  -5.059  9.600   0.70 15.68 ?  20  ASN   A H    1 
ATOM   530  H  H    B ASN   A 1 20  ? 7.928  -4.955  10.124  0.30 15.86 ?  20  ASN   A H    1 
ATOM   531  H  HA   A ASN   A 1 20  ? 8.763  -3.375  7.740   0.70 17.16 ?  20  ASN   A HA   1 
ATOM   532  H  HA   B ASN   A 1 20  ? 8.749  -3.265  8.238   0.30 17.03 ?  20  ASN   A HA   1 
ATOM   533  H  HB2  A ASN   A 1 20  ? 6.498  -3.780  7.655   0.70 17.93 ?  20  ASN   A HB2  1 
ATOM   534  H  HB2  B ASN   A 1 20  ? 6.503  -3.558  8.251   0.30 17.77 ?  20  ASN   A HB2  1 
ATOM   535  H  HB3  A ASN   A 1 20  ? 6.328  -3.364  9.177   0.70 17.93 ?  20  ASN   A HB3  1 
ATOM   536  H  HB3  B ASN   A 1 20  ? 6.415  -3.313  9.819   0.30 17.77 ?  20  ASN   A HB3  1 
ATOM   537  H  HD21 A ASN   A 1 20  ? 7.173  -0.394  6.772   0.70 20.13 ?  20  ASN   A HD21 1 
ATOM   538  H  HD21 B ASN   A 1 20  ? 7.060  -0.152  7.593   0.30 18.68 ?  20  ASN   A HD21 1 
ATOM   539  H  HD22 A ASN   A 1 20  ? 7.991  -1.638  6.743   0.70 20.13 ?  20  ASN   A HD22 1 
ATOM   540  H  HD22 B ASN   A 1 20  ? 7.785  -1.422  7.312   0.30 18.68 ?  20  ASN   A HD22 1 
ATOM   541  N  N    A ALA   A 1 21  ? 10.053 -1.831  9.186   0.70 16.01 ?  21  ALA   A N    1 
ATOM   542  N  N    B ALA   A 1 21  ? 10.154 -1.764  9.565   0.30 15.28 ?  21  ALA   A N    1 
ATOM   543  C  CA   A ALA   A 1 21  ? 10.749 -0.941  10.108  0.70 16.51 ?  21  ALA   A CA   1 
ATOM   544  C  CA   B ALA   A 1 21  ? 10.845 -0.726  10.307  0.30 15.48 ?  21  ALA   A CA   1 
ATOM   545  C  C    A ALA   A 1 21  ? 11.723 -0.047  9.357   0.70 16.12 ?  21  ALA   A C    1 
ATOM   546  C  C    B ALA   A 1 21  ? 11.888 -0.099  9.404   0.30 15.11 ?  21  ALA   A C    1 
ATOM   547  O  O    A ALA   A 1 21  ? 12.187 -0.380  8.263   0.70 15.94 ?  21  ALA   A O    1 
ATOM   548  O  O    B ALA   A 1 21  ? 12.457 -0.765  8.537   0.30 15.38 ?  21  ALA   A O    1 
ATOM   549  C  CB   A ALA   A 1 21  ? 11.499 -1.729  11.186  0.70 17.24 ?  21  ALA   A CB   1 
ATOM   550  C  CB   B ALA   A 1 21  ? 11.514 -1.288  11.567  0.30 16.27 ?  21  ALA   A CB   1 
ATOM   551  H  H    A ALA   A 1 21  ? 10.445 -1.954  8.432   0.70 19.20 ?  21  ALA   A H    1 
ATOM   552  H  H    B ALA   A 1 21  ? 10.547 -2.003  8.838   0.30 18.32 ?  21  ALA   A H    1 
ATOM   553  H  HA   A ALA   A 1 21  ? 10.092 -0.378  10.549  0.70 19.79 ?  21  ALA   A HA   1 
ATOM   554  H  HA   B ALA   A 1 21  ? 10.215 -0.041  10.574  0.30 18.57 ?  21  ALA   A HA   1 
ATOM   555  H  HB1  A ALA   A 1 21  ? 11.932 -1.103  11.785  0.70 20.67 ?  21  ALA   A HB1  1 
ATOM   556  H  HB1  B ALA   A 1 21  ? 11.961 -0.565  12.035  0.30 19.51 ?  21  ALA   A HB1  1 
ATOM   557  H  HB2  A ALA   A 1 21  ? 10.860 -2.270  11.681  0.70 20.67 ?  21  ALA   A HB2  1 
ATOM   558  H  HB2  B ALA   A 1 21  ? 10.834 -1.679  12.138  0.30 19.51 ?  21  ALA   A HB2  1 
ATOM   559  H  HB3  A ALA   A 1 21  ? 12.156 -2.298  10.762  0.70 20.67 ?  21  ALA   A HB3  1 
ATOM   560  H  HB3  B ALA   A 1 21  ? 12.158 -1.965  11.308  0.30 19.51 ?  21  ALA   A HB3  1 
ATOM   561  N  N    A ASP   A 1 22  ? 12.020 1.099   9.981   0.70 16.19 ?  22  ASP   A N    1 
ATOM   562  N  N    B ASP   A 1 22  ? 12.092 1.199   9.592   0.30 14.66 ?  22  ASP   A N    1 
ATOM   563  C  CA   A ASP   A 1 22  ? 13.052 2.028   9.528   0.70 16.10 ?  22  ASP   A CA   1 
ATOM   564  C  CA   B ASP   A 1 22  ? 13.262 1.864   9.044   0.30 14.47 ?  22  ASP   A CA   1 
ATOM   565  C  C    A ASP   A 1 22  ? 14.381 1.561   10.115  0.70 14.93 ?  22  ASP   A C    1 
ATOM   566  C  C    B ASP   A 1 22  ? 14.508 1.247   9.669   0.30 13.40 ?  22  ASP   A C    1 
ATOM   567  O  O    A ASP   A 1 22  ? 14.562 1.568   11.337  0.70 15.70 ?  22  ASP   A O    1 
ATOM   568  O  O    B ASP   A 1 22  ? 14.626 1.172   10.895  0.30 13.28 ?  22  ASP   A O    1 
ATOM   569  C  CB   A ASP   A 1 22  ? 12.700 3.440   9.995   0.70 17.82 ?  22  ASP   A CB   1 
ATOM   570  C  CB   B ASP   A 1 22  ? 13.175 3.349   9.399   0.30 15.63 ?  22  ASP   A CB   1 
ATOM   571  C  CG   A ASP   A 1 22  ? 13.736 4.485   9.588   0.70 20.03 ?  22  ASP   A CG   1 
ATOM   572  C  CG   B ASP   A 1 22  ? 14.196 4.193   8.679   0.30 16.09 ?  22  ASP   A CG   1 
ATOM   573  O  OD1  A ASP   A 1 22  ? 14.843 4.123   9.137   0.70 20.85 ?  22  ASP   A OD1  1 
ATOM   574  O  OD1  B ASP   A 1 22  ? 15.219 3.642   8.226   0.30 15.57 ?  22  ASP   A OD1  1 
ATOM   575  O  OD2  A ASP   A 1 22  ? 13.433 5.690   9.725   0.70 21.82 -1 22  ASP   A OD2  1 
ATOM   576  O  OD2  B ASP   A 1 22  ? 13.977 5.418   8.575   0.30 17.14 -1 22  ASP   A OD2  1 
ATOM   577  H  H    A ASP   A 1 22  ? 11.605 1.373   10.687  0.70 19.42 ?  22  ASP   A H    1 
ATOM   578  H  H    B ASP   A 1 22  ? 11.556 1.716   10.024  0.30 17.58 ?  22  ASP   A H    1 
ATOM   579  H  HA   A ASP   A 1 22  ? 13.109 2.017   8.560   0.70 19.31 ?  22  ASP   A HA   1 
ATOM   580  H  HA   B ASP   A 1 22  ? 13.291 1.754   8.078   0.30 17.35 ?  22  ASP   A HA   1 
ATOM   581  H  HB2  A ASP   A 1 22  ? 11.842 3.694   9.612   0.70 21.36 ?  22  ASP   A HB2  1 
ATOM   582  H  HB2  B ASP   A 1 22  ? 12.302 3.682   9.154   0.30 18.74 ?  22  ASP   A HB2  1 
ATOM   583  H  HB3  A ASP   A 1 22  ? 12.634 3.443   10.965  0.70 21.36 ?  22  ASP   A HB3  1 
ATOM   584  H  HB3  B ASP   A 1 22  ? 13.318 3.449   10.352  0.30 18.74 ?  22  ASP   A HB3  1 
ATOM   585  N  N    A ILE   A 1 23  ? 15.301 1.140   9.243   0.70 14.54 ?  23  ILE   A N    1 
ATOM   586  N  N    B ILE   A 1 23  ? 15.433 0.779   8.825   0.30 13.13 ?  23  ILE   A N    1 
ATOM   587  C  CA   A ILE   A 1 23  ? 16.552 0.532   9.693   0.70 14.05 ?  23  ILE   A CA   1 
ATOM   588  C  CA   B ILE   A 1 23  ? 16.654 0.162   9.340   0.30 12.65 ?  23  ILE   A CA   1 
ATOM   589  C  C    A ILE   A 1 23  ? 17.349 1.485   10.573  0.70 14.22 ?  23  ILE   A C    1 
ATOM   590  C  C    B ILE   A 1 23  ? 17.411 1.132   10.233  0.30 13.07 ?  23  ILE   A C    1 
ATOM   591  O  O    A ILE   A 1 23  ? 18.077 1.047   11.474  0.70 14.94 ?  23  ILE   A O    1 
ATOM   592  O  O    B ILE   A 1 23  ? 18.090 0.716   11.180  0.30 13.22 ?  23  ILE   A O    1 
ATOM   593  C  CB   A ILE   A 1 23  ? 17.360 0.018   8.480   0.70 13.68 ?  23  ILE   A CB   1 
ATOM   594  C  CB   B ILE   A 1 23  ? 17.542 -0.391  8.203   0.30 12.30 ?  23  ILE   A CB   1 
ATOM   595  C  CG1  A ILE   A 1 23  ? 18.511 -0.882  8.935   0.70 13.81 ?  23  ILE   A CG1  1 
ATOM   596  C  CG1  B ILE   A 1 23  ? 18.613 -1.319  8.786   0.30 12.02 ?  23  ILE   A CG1  1 
ATOM   597  C  CG2  A ILE   A 1 23  ? 17.859 1.175   7.619   0.70 13.64 ?  23  ILE   A CG2  1 
ATOM   598  C  CG2  B ILE   A 1 23  ? 18.192 0.741   7.409   0.30 12.05 ?  23  ILE   A CG2  1 
ATOM   599  C  CD1  A ILE   A 1 23  ? 19.182 -1.625  7.795   0.70 14.02 ?  23  ILE   A CD1  1 
ATOM   600  C  CD1  B ILE   A 1 23  ? 19.570 -1.885  7.764   0.30 11.73 ?  23  ILE   A CD1  1 
ATOM   601  H  H    A ILE   A 1 23  ? 15.219 1.194   8.391   0.70 17.43 ?  23  ILE   A H    1 
ATOM   602  H  H    B ILE   A 1 23  ? 15.377 0.802   7.976   0.30 15.74 ?  23  ILE   A H    1 
ATOM   603  H  HA   A ILE   A 1 23  ? 16.334 -0.239  10.236  0.70 16.84 ?  23  ILE   A HA   1 
ATOM   604  H  HA   B ILE   A 1 23  ? 16.399 -0.593  9.889   0.30 15.17 ?  23  ILE   A HA   1 
ATOM   605  H  HB   A ILE   A 1 23  ? 16.764 -0.519  7.934   0.70 16.41 ?  23  ILE   A HB   1 
ATOM   606  H  HB   B ILE   A 1 23  ? 16.987 -0.909  7.601   0.30 14.74 ?  23  ILE   A HB   1 
ATOM   607  H  HG12 A ILE   A 1 23  ? 19.184 -0.338  9.371   0.70 16.55 ?  23  ILE   A HG12 1 
ATOM   608  H  HG12 B ILE   A 1 23  ? 19.139 -0.827  9.435   0.30 14.41 ?  23  ILE   A HG12 1 
ATOM   609  H  HG13 A ILE   A 1 23  ? 18.166 -1.543  9.556   0.70 16.55 ?  23  ILE   A HG13 1 
ATOM   610  H  HG13 B ILE   A 1 23  ? 18.176 -2.069  9.221   0.30 14.41 ?  23  ILE   A HG13 1 
ATOM   611  H  HG21 A ILE   A 1 23  ? 18.220 0.823   6.790   0.70 16.35 ?  23  ILE   A HG21 1 
ATOM   612  H  HG21 B ILE   A 1 23  ? 18.551 0.380   6.580   0.30 14.44 ?  23  ILE   A HG21 1 
ATOM   613  H  HG22 A ILE   A 1 23  ? 17.111 1.767   7.424   0.70 16.35 ?  23  ILE   A HG22 1 
ATOM   614  H  HG22 B ILE   A 1 23  ? 17.522 1.411   7.212   0.30 14.44 ?  23  ILE   A HG22 1 
ATOM   615  H  HG23 A ILE   A 1 23  ? 18.544 1.660   8.101   0.70 16.35 ?  23  ILE   A HG23 1 
ATOM   616  H  HG23 B ILE   A 1 23  ? 18.908 1.129   7.935   0.30 14.44 ?  23  ILE   A HG23 1 
ATOM   617  H  HD11 A ILE   A 1 23  ? 19.850 -2.225  8.160   0.70 16.81 ?  23  ILE   A HD11 1 
ATOM   618  H  HD11 B ILE   A 1 23  ? 20.109 -2.574  8.187   0.30 14.06 ?  23  ILE   A HD11 1 
ATOM   619  H  HD12 A ILE   A 1 23  ? 18.510 -2.132  7.311   0.70 16.81 ?  23  ILE   A HD12 1 
ATOM   620  H  HD12 B ILE   A 1 23  ? 19.059 -2.264  7.035   0.30 14.06 ?  23  ILE   A HD12 1 
ATOM   621  H  HD13 A ILE   A 1 23  ? 19.600 -0.982  7.202   0.70 16.81 ?  23  ILE   A HD13 1 
ATOM   622  H  HD13 B ILE   A 1 23  ? 20.140 -1.173  7.438   0.30 14.06 ?  23  ILE   A HD13 1 
ATOM   623  N  N    A VAL   A 1 24  ? 17.221 2.793   10.343  0.70 14.51 ?  24  VAL   A N    1 
ATOM   624  N  N    B VAL   A 1 24  ? 17.310 2.432   9.950   0.30 13.80 ?  24  VAL   A N    1 
ATOM   625  C  CA   A VAL   A 1 24  ? 17.913 3.762   11.190  0.70 15.80 ?  24  VAL   A CA   1 
ATOM   626  C  CA   B VAL   A 1 24  ? 17.941 3.434   10.803  0.30 14.88 ?  24  VAL   A CA   1 
ATOM   627  C  C    A VAL   A 1 24  ? 17.389 3.683   12.617  0.70 16.12 ?  24  VAL   A C    1 
ATOM   628  C  C    B VAL   A 1 24  ? 17.314 3.417   12.191  0.30 15.87 ?  24  VAL   A C    1 
ATOM   629  O  O    A VAL   A 1 24  ? 18.162 3.604   13.583  0.70 16.48 ?  24  VAL   A O    1 
ATOM   630  O  O    B VAL   A 1 24  ? 18.017 3.443   13.208  0.30 16.64 ?  24  VAL   A O    1 
ATOM   631  C  CB   A VAL   A 1 24  ? 17.766 5.180   10.610  0.70 16.78 ?  24  VAL   A CB   1 
ATOM   632  C  CB   B VAL   A 1 24  ? 17.854 4.823   10.141  0.30 15.25 ?  24  VAL   A CB   1 
ATOM   633  C  CG1  A VAL   A 1 24  ? 18.247 6.223   11.614  0.70 17.63 ?  24  VAL   A CG1  1 
ATOM   634  C  CG1  B VAL   A 1 24  ? 18.541 5.867   11.001  0.30 15.92 ?  24  VAL   A CG1  1 
ATOM   635  C  CG2  A VAL   A 1 24  ? 18.525 5.297   9.297   0.70 17.65 ?  24  VAL   A CG2  1 
ATOM   636  C  CG2  B VAL   A 1 24  ? 18.466 4.778   8.750   0.30 15.05 ?  24  VAL   A CG2  1 
ATOM   637  H  H    A VAL   A 1 24  ? 16.747 3.139   9.711   0.70 17.40 ?  24  VAL   A H    1 
ATOM   638  H  H    B VAL   A 1 24  ? 16.885 2.756   9.279   0.30 16.55 ?  24  VAL   A H    1 
ATOM   639  H  HA   A VAL   A 1 24  ? 18.856 3.546   11.203  0.70 18.94 ?  24  VAL   A HA   1 
ATOM   640  H  HA   B VAL   A 1 24  ? 18.880 3.217   10.902  0.30 17.84 ?  24  VAL   A HA   1 
ATOM   641  H  HB   A VAL   A 1 24  ? 16.830 5.352   10.422  0.70 20.12 ?  24  VAL   A HB   1 
ATOM   642  H  HB   B VAL   A 1 24  ? 16.921 5.076   10.048  0.30 18.28 ?  24  VAL   A HB   1 
ATOM   643  H  HG11 A VAL   A 1 24  ? 18.409 7.056   11.146  0.70 21.15 ?  24  VAL   A HG11 1 
ATOM   644  H  HG11 B VAL   A 1 24  ? 18.660 6.679   10.483  0.30 19.08 ?  24  VAL   A HG11 1 
ATOM   645  H  HG12 A VAL   A 1 24  ? 17.564 6.349   12.288  0.70 21.15 ?  24  VAL   A HG12 1 
ATOM   646  H  HG12 B VAL   A 1 24  ? 17.982 6.048   11.772  0.30 19.08 ?  24  VAL   A HG12 1 
ATOM   647  H  HG13 A VAL   A 1 24  ? 19.068 5.908   12.022  0.70 21.15 ?  24  VAL   A HG13 1 
ATOM   648  H  HG13 B VAL   A 1 24  ? 19.403 5.527   11.285  0.30 19.08 ?  24  VAL   A HG13 1 
ATOM   649  H  HG21 A VAL   A 1 24  ? 18.422 6.198   8.948   0.70 21.16 ?  24  VAL   A HG21 1 
ATOM   650  H  HG21 B VAL   A 1 24  ? 18.598 5.684   8.432   0.30 18.04 ?  24  VAL   A HG21 1 
ATOM   651  H  HG22 A VAL   A 1 24  ? 19.466 5.114   9.458   0.70 21.16 ?  24  VAL   A HG22 1 
ATOM   652  H  HG22 B VAL   A 1 24  ? 19.318 4.317   8.797   0.30 18.04 ?  24  VAL   A HG22 1 
ATOM   653  H  HG23 A VAL   A 1 24  ? 18.169 4.655   8.663   0.70 21.16 ?  24  VAL   A HG23 1 
ATOM   654  H  HG23 B VAL   A 1 24  ? 17.867 4.301   8.156   0.30 18.04 ?  24  VAL   A HG23 1 
ATOM   655  N  N    A GLU   A 1 25  ? 16.064 3.710   12.769  0.70 16.94 ?  25  GLU   A N    1 
ATOM   656  N  N    B GLU   A 1 25  ? 15.982 3.351   12.256  0.30 16.40 ?  25  GLU   A N    1 
ATOM   657  C  CA   A GLU   A 1 25  ? 15.473 3.650   14.101  0.70 18.23 ?  25  GLU   A CA   1 
ATOM   658  C  CA   B GLU   A 1 25  ? 15.310 3.293   13.551  0.30 17.27 ?  25  GLU   A CA   1 
ATOM   659  C  C    A GLU   A 1 25  ? 15.707 2.291   14.745  0.70 17.09 ?  25  GLU   A C    1 
ATOM   660  C  C    B GLU   A 1 25  ? 15.598 1.978   14.268  0.30 17.42 ?  25  GLU   A C    1 
ATOM   661  O  O    A GLU   A 1 25  ? 15.934 2.205   15.959  0.70 17.84 ?  25  GLU   A O    1 
ATOM   662  O  O    B GLU   A 1 25  ? 15.800 1.963   15.488  0.30 17.76 ?  25  GLU   A O    1 
ATOM   663  C  CB   A GLU   A 1 25  ? 13.984 3.989   14.027  0.70 20.77 ?  25  GLU   A CB   1 
ATOM   664  C  CB   B GLU   A 1 25  ? 13.808 3.516   13.376  0.30 18.37 ?  25  GLU   A CB   1 
ATOM   665  C  CG   A GLU   A 1 25  ? 13.723 5.445   13.662  0.70 23.89 ?  25  GLU   A CG   1 
ATOM   666  C  CG   B GLU   A 1 25  ? 13.458 4.902   12.854  0.30 20.22 ?  25  GLU   A CG   1 
ATOM   667  C  CD   A GLU   A 1 25  ? 14.523 6.420   14.512  0.70 26.33 ?  25  GLU   A CD   1 
ATOM   668  C  CD   B GLU   A 1 25  ? 13.941 6.009   13.769  0.30 21.81 ?  25  GLU   A CD   1 
ATOM   669  O  OE1  A GLU   A 1 25  ? 14.571 6.238   15.747  0.70 27.18 ?  25  GLU   A OE1  1 
ATOM   670  O  OE1  B GLU   A 1 25  ? 13.914 5.813   15.003  0.30 22.62 ?  25  GLU   A OE1  1 
ATOM   671  O  OE2  A GLU   A 1 25  ? 15.122 7.355   13.940  0.70 27.42 -1 25  GLU   A OE2  1 
ATOM   672  O  OE2  B GLU   A 1 25  ? 14.354 7.068   13.255  0.30 22.48 -1 25  GLU   A OE2  1 
ATOM   673  H  H    A GLU   A 1 25  ? 15.493 3.770   12.125  0.70 20.31 ?  25  GLU   A H    1 
ATOM   674  H  H    B GLU   A 1 25  ? 15.458 3.342   11.575  0.30 19.67 ?  25  GLU   A H    1 
ATOM   675  H  HA   A GLU   A 1 25  ? 15.908 4.304   14.664  0.70 21.85 ?  25  GLU   A HA   1 
ATOM   676  H  HA   B GLU   A 1 25  ? 15.652 4.008   14.106  0.30 20.71 ?  25  GLU   A HA   1 
ATOM   677  H  HB2  A GLU   A 1 25  ? 13.562 3.435   13.346  0.70 24.90 ?  25  GLU   A HB2  1 
ATOM   678  H  HB2  B GLU   A 1 25  ? 13.463 2.867   12.744  0.30 22.03 ?  25  GLU   A HB2  1 
ATOM   679  H  HB3  A GLU   A 1 25  ? 13.572 3.819   14.888  0.70 24.90 ?  25  GLU   A HB3  1 
ATOM   680  H  HB3  B GLU   A 1 25  ? 13.372 3.405   14.235  0.30 22.03 ?  25  GLU   A HB3  1 
ATOM   681  H  HG2  A GLU   A 1 25  ? 13.978 5.588   12.740  0.70 28.65 ?  25  GLU   A HG2  1 
ATOM   682  H  HG2  B GLU   A 1 25  ? 13.876 5.030   11.988  0.30 24.24 ?  25  GLU   A HG2  1 
ATOM   683  H  HG3  A GLU   A 1 25  ? 12.780 5.636   13.784  0.70 28.65 ?  25  GLU   A HG3  1 
ATOM   684  H  HG3  B GLU   A 1 25  ? 12.495 4.979   12.774  0.30 24.24 ?  25  GLU   A HG3  1 
ATOM   685  N  N    A GLU   A 1 26  ? 15.675 1.220   13.948  0.70 16.97 ?  26  GLU   A N    1 
ATOM   686  N  N    B GLU   A 1 26  ? 15.622 0.862   13.534  0.30 17.13 ?  26  GLU   A N    1 
ATOM   687  C  CA   A GLU   A 1 26  ? 15.957 -0.108  14.483  0.70 17.08 ?  26  GLU   A CA   1 
ATOM   688  C  CA   B GLU   A 1 26  ? 16.012 -0.406  14.143  0.30 17.40 ?  26  GLU   A CA   1 
ATOM   689  C  C    A GLU   A 1 26  ? 17.381 -0.187  15.019  0.70 16.33 ?  26  GLU   A C    1 
ATOM   690  C  C    B GLU   A 1 26  ? 17.423 -0.332  14.709  0.30 16.91 ?  26  GLU   A C    1 
ATOM   691  O  O    A GLU   A 1 26  ? 17.616 -0.693  16.122  0.70 17.03 ?  26  GLU   A O    1 
ATOM   692  O  O    B GLU   A 1 26  ? 17.688 -0.830  15.809  0.30 16.82 ?  26  GLU   A O    1 
ATOM   693  C  CB   A GLU   A 1 26  ? 15.740 -1.165  13.400  0.70 18.62 ?  26  GLU   A CB   1 
ATOM   694  C  CB   B GLU   A 1 26  ? 15.926 -1.540  13.119  0.30 18.22 ?  26  GLU   A CB   1 
ATOM   695  C  CG   A GLU   A 1 26  ? 14.307 -1.624  13.224  0.70 22.30 ?  26  GLU   A CG   1 
ATOM   696  C  CG   B GLU   A 1 26  ? 14.554 -2.170  12.985  0.30 18.67 ?  26  GLU   A CG   1 
ATOM   697  C  CD   A GLU   A 1 26  ? 13.788 -2.429  14.395  0.70 24.62 ?  26  GLU   A CD   1 
ATOM   698  C  CD   B GLU   A 1 26  ? 14.021 -2.757  14.288  0.30 18.53 ?  26  GLU   A CD   1 
ATOM   699  O  OE1  A GLU   A 1 26  ? 14.432 -3.429  14.777  0.70 25.32 ?  26  GLU   A OE1  1 
ATOM   700  O  OE1  B GLU   A 1 26  ? 14.366 -3.913  14.646  0.30 18.31 ?  26  GLU   A OE1  1 
ATOM   701  O  OE2  A GLU   A 1 26  ? 12.729 -2.047  14.931  0.70 26.11 -1 26  GLU   A OE2  1 
ATOM   702  O  OE2  B GLU   A 1 26  ? 13.245 -2.056  14.957  0.30 18.11 -1 26  GLU   A OE2  1 
ATOM   703  H  H    A GLU   A 1 26  ? 15.501 1.242   13.106  0.70 20.35 ?  26  GLU   A H    1 
ATOM   704  H  H    B GLU   A 1 26  ? 15.415 0.814   12.701  0.30 20.54 ?  26  GLU   A H    1 
ATOM   705  H  HA   A GLU   A 1 26  ? 15.347 -0.290  15.211  0.70 20.48 ?  26  GLU   A HA   1 
ATOM   706  H  HA   B GLU   A 1 26  ? 15.410 -0.602  14.877  0.30 20.87 ?  26  GLU   A HA   1 
ATOM   707  H  HB2  A GLU   A 1 26  ? 16.033 -0.798  12.548  0.70 22.33 ?  26  GLU   A HB2  1 
ATOM   708  H  HB2  B GLU   A 1 26  ? 16.176 -1.189  12.246  0.30 21.85 ?  26  GLU   A HB2  1 
ATOM   709  H  HB3  A GLU   A 1 26  ? 16.278 -1.941  13.618  0.70 22.33 ?  26  GLU   A HB3  1 
ATOM   710  H  HB3  B GLU   A 1 26  ? 16.545 -2.240  13.375  0.30 21.85 ?  26  GLU   A HB3  1 
ATOM   711  H  HG2  A GLU   A 1 26  ? 13.733 -0.853  13.158  0.70 26.74 ?  26  GLU   A HG2  1 
ATOM   712  H  HG2  B GLU   A 1 26  ? 13.947 -1.492  12.640  0.30 22.39 ?  26  GLU   A HG2  1 
ATOM   713  H  HG3  A GLU   A 1 26  ? 14.246 -2.160  12.416  0.70 26.74 ?  26  GLU   A HG3  1 
ATOM   714  H  HG3  B GLU   A 1 26  ? 14.608 -2.913  12.376  0.30 22.39 ?  26  GLU   A HG3  1 
ATOM   715  N  N    A ALA   A 1 27  ? 18.351 0.305   14.245  0.70 15.31 ?  27  ALA   A N    1 
ATOM   716  N  N    B ALA   A 1 27  ? 18.348 0.274   13.964  0.30 16.41 ?  27  ALA   A N    1 
ATOM   717  C  CA   A ALA   A 1 27  ? 19.742 0.251   14.687  0.70 15.53 ?  27  ALA   A CA   1 
ATOM   718  C  CA   B ALA   A 1 27  ? 19.727 0.355   14.434  0.30 16.52 ?  27  ALA   A CA   1 
ATOM   719  C  C    A ALA   A 1 27  ? 19.942 1.043   15.973  0.70 16.85 ?  27  ALA   A C    1 
ATOM   720  C  C    B ALA   A 1 27  ? 19.831 1.228   15.680  0.30 17.21 ?  27  ALA   A C    1 
ATOM   721  O  O    A ALA   A 1 27  ? 20.620 0.580   16.897  0.70 17.13 ?  27  ALA   A O    1 
ATOM   722  O  O    B ALA   A 1 27  ? 20.490 0.855   16.657  0.30 17.31 ?  27  ALA   A O    1 
ATOM   723  C  CB   A ALA   A 1 27  ? 20.670 0.763   13.582  0.70 15.21 ?  27  ALA   A CB   1 
ATOM   724  C  CB   B ALA   A 1 27  ? 20.631 0.882   13.320  0.30 16.19 ?  27  ALA   A CB   1 
ATOM   725  H  H    A ALA   A 1 27  ? 18.232 0.666   13.473  0.70 18.36 ?  27  ALA   A H    1 
ATOM   726  H  H    B ALA   A 1 27  ? 18.202 0.634   13.196  0.30 19.68 ?  27  ALA   A H    1 
ATOM   727  H  HA   A ALA   A 1 27  ? 19.976 -0.671  14.863  0.70 18.62 ?  27  ALA   A HA   1 
ATOM   728  H  HA   B ALA   A 1 27  ? 20.027 -0.536  14.666  0.30 19.81 ?  27  ALA   A HA   1 
ATOM   729  H  HB1  A ALA   A 1 27  ? 21.589 0.718   13.896  0.70 18.24 ?  27  ALA   A HB1  1 
ATOM   730  H  HB1  B ALA   A 1 27  ? 21.541 0.925   13.651  0.30 19.41 ?  27  ALA   A HB1  1 
ATOM   731  H  HB2  A ALA   A 1 27  ? 20.566 0.205   12.795  0.70 18.24 ?  27  ALA   A HB2  1 
ATOM   732  H  HB2  B ALA   A 1 27  ? 20.582 0.278   12.562  0.30 19.41 ?  27  ALA   A HB2  1 
ATOM   733  H  HB3  A ALA   A 1 27  ? 20.439 1.681   13.370  0.70 18.24 ?  27  ALA   A HB3  1 
ATOM   734  H  HB3  B ALA   A 1 27  ? 20.329 1.766   13.059  0.30 19.41 ?  27  ALA   A HB3  1 
ATOM   735  N  N    A LYS   A 1 28  ? 19.348 2.235   16.058  0.70 18.80 ?  28  LYS   A N    1 
ATOM   736  N  N    B LYS   A 1 28  ? 19.175 2.391   15.668  0.30 18.34 ?  28  LYS   A N    1 
ATOM   737  C  CA   A LYS   A 1 28  ? 19.493 3.037   17.268  0.70 21.44 ?  28  LYS   A CA   1 
ATOM   738  C  CA   B LYS   A 1 28  ? 19.287 3.313   16.794  0.30 19.94 ?  28  LYS   A CA   1 
ATOM   739  C  C    A LYS   A 1 28  ? 18.924 2.321   18.487  0.70 22.68 ?  28  LYS   A C    1 
ATOM   740  C  C    B LYS   A 1 28  ? 18.824 2.678   18.097  0.30 21.25 ?  28  LYS   A C    1 
ATOM   741  O  O    A LYS   A 1 28  ? 19.467 2.449   19.590  0.70 23.81 ?  28  LYS   A O    1 
ATOM   742  O  O    B LYS   A 1 28  ? 19.320 3.039   19.171  0.30 21.29 ?  28  LYS   A O    1 
ATOM   743  C  CB   A LYS   A 1 28  ? 18.851 4.413   17.074  0.70 23.10 ?  28  LYS   A CB   1 
ATOM   744  C  CB   B LYS   A 1 28  ? 18.485 4.585   16.519  0.30 20.79 ?  28  LYS   A CB   1 
ATOM   745  C  CG   A LYS   A 1 28  ? 19.658 5.331   16.165  0.70 24.79 ?  28  LYS   A CG   1 
ATOM   746  C  CG   B LYS   A 1 28  ? 19.082 5.476   15.446  0.30 21.64 ?  28  LYS   A CG   1 
ATOM   747  C  CD   A LYS   A 1 28  ? 19.191 6.774   16.236  0.70 27.13 ?  28  LYS   A CD   1 
ATOM   748  C  CD   B LYS   A 1 28  ? 18.288 6.763   15.303  0.30 22.44 ?  28  LYS   A CD   1 
ATOM   749  C  CE   A LYS   A 1 28  ? 17.884 6.973   15.497  0.70 28.90 ?  28  LYS   A CE   1 
ATOM   750  C  CE   B LYS   A 1 28  ? 18.874 7.667   14.232  0.30 23.11 ?  28  LYS   A CE   1 
ATOM   751  N  NZ   A LYS   A 1 28  ? 17.505 8.410   15.439  0.70 29.96 ?  28  LYS   A NZ   1 
ATOM   752  N  NZ   B LYS   A 1 28  ? 18.178 8.983   14.161  0.30 23.32 ?  28  LYS   A NZ   1 
ATOM   753  H  H    A LYS   A 1 28  ? 18.869 2.591   15.444  0.70 22.54 ?  28  LYS   A H    1 
ATOM   754  H  H    B LYS   A 1 28  ? 18.667 2.665   15.033  0.30 21.99 ?  28  LYS   A H    1 
ATOM   755  H  HA   A LYS   A 1 28  ? 20.436 3.180   17.437  0.70 25.71 ?  28  LYS   A HA   1 
ATOM   756  H  HA   B LYS   A 1 28  ? 20.214 3.563   16.906  0.30 23.92 ?  28  LYS   A HA   1 
ATOM   757  H  HB2  A LYS   A 1 28  ? 17.975 4.303   16.676  0.70 27.70 ?  28  LYS   A HB2  1 
ATOM   758  H  HB2  B LYS   A 1 28  ? 17.592 4.337   16.233  0.30 24.94 ?  28  LYS   A HB2  1 
ATOM   759  H  HB3  A LYS   A 1 28  ? 18.771 4.852   17.935  0.70 27.70 ?  28  LYS   A HB3  1 
ATOM   760  H  HB3  B LYS   A 1 28  ? 18.434 5.105   17.337  0.30 24.94 ?  28  LYS   A HB3  1 
ATOM   761  H  HG2  A LYS   A 1 28  ? 20.590 5.305   16.431  0.70 29.73 ?  28  LYS   A HG2  1 
ATOM   762  H  HG2  B LYS   A 1 28  ? 19.992 5.705   15.690  0.30 25.95 ?  28  LYS   A HG2  1 
ATOM   763  H  HG3  A LYS   A 1 28  ? 19.565 5.032   15.247  0.70 29.73 ?  28  LYS   A HG3  1 
ATOM   764  H  HG3  B LYS   A 1 28  ? 19.071 5.013   14.594  0.30 25.95 ?  28  LYS   A HG3  1 
ATOM   765  H  HD2  A LYS   A 1 28  ? 19.056 7.023   17.164  0.70 32.54 ?  28  LYS   A HD2  1 
ATOM   766  H  HD2  B LYS   A 1 28  ? 17.374 6.550   15.056  0.30 26.91 ?  28  LYS   A HD2  1 
ATOM   767  H  HD3  A LYS   A 1 28  ? 19.860 7.348   15.830  0.70 32.54 ?  28  LYS   A HD3  1 
ATOM   768  H  HD3  B LYS   A 1 28  ? 18.303 7.243   16.147  0.30 26.91 ?  28  LYS   A HD3  1 
ATOM   769  H  HE2  A LYS   A 1 28  ? 17.978 6.645   14.589  0.70 34.66 ?  28  LYS   A HE2  1 
ATOM   770  H  HE2  B LYS   A 1 28  ? 19.808 7.830   14.432  0.30 27.72 ?  28  LYS   A HE2  1 
ATOM   771  H  HE3  A LYS   A 1 28  ? 17.180 6.490   15.957  0.70 34.66 ?  28  LYS   A HE3  1 
ATOM   772  H  HE3  B LYS   A 1 28  ? 18.792 7.233   13.369  0.30 27.72 ?  28  LYS   A HE3  1 
ATOM   773  H  HZ1  A LYS   A 1 28  ? 16.737 8.504   15.001  0.70 35.94 ?  28  LYS   A HZ1  1 
ATOM   774  H  HZ1  B LYS   A 1 28  ? 18.544 9.486   13.525  0.30 27.97 ?  28  LYS   A HZ1  1 
ATOM   775  H  HZ2  A LYS   A 1 28  ? 17.411 8.733   16.263  0.70 35.94 ?  28  LYS   A HZ2  1 
ATOM   776  H  HZ2  B LYS   A 1 28  ? 17.316 8.861   13.974  0.30 27.97 ?  28  LYS   A HZ2  1 
ATOM   777  H  HZ3  A LYS   A 1 28  ? 18.138 8.874   15.017  0.70 35.94 ?  28  LYS   A HZ3  1 
ATOM   778  H  HZ3  B LYS   A 1 28  ? 18.248 9.405   14.941  0.30 27.97 ?  28  LYS   A HZ3  1 
ATOM   779  N  N    A LYS   A 1 29  ? 17.853 1.548   18.309  0.70 23.52 ?  29  LYS   A N    1 
ATOM   780  N  N    B LYS   A 1 29  ? 17.883 1.737   18.031  0.30 22.64 ?  29  LYS   A N    1 
ATOM   781  C  CA   A LYS   A 1 29  ? 17.246 0.835   19.430  0.70 25.09 ?  29  LYS   A CA   1 
ATOM   782  C  CA   B LYS   A 1 29  ? 17.325 1.138   19.236  0.30 24.30 ?  29  LYS   A CA   1 
ATOM   783  C  C    A LYS   A 1 29  ? 18.055 -0.401  19.811  0.70 24.92 ?  29  LYS   A C    1 
ATOM   784  C  C    B LYS   A 1 29  ? 18.072 -0.123  19.656  0.30 24.23 ?  29  LYS   A C    1 
ATOM   785  O  O    A LYS   A 1 29  ? 18.333 -0.631  20.994  0.70 25.81 ?  29  LYS   A O    1 
ATOM   786  O  O    B LYS   A 1 29  ? 18.393 -0.292  20.837  0.30 24.85 ?  29  LYS   A O    1 
ATOM   787  C  CB   A LYS   A 1 29  ? 15.815 0.430   19.071  0.70 27.52 ?  29  LYS   A CB   1 
ATOM   788  C  CB   B LYS   A 1 29  ? 15.842 0.820   19.021  0.30 25.89 ?  29  LYS   A CB   1 
ATOM   789  C  CG   A LYS   A 1 29  ? 15.063 -0.269  20.195  0.70 30.19 ?  29  LYS   A CG   1 
ATOM   790  C  CG   B LYS   A 1 29  ? 15.116 0.385   20.280  0.30 27.45 ?  29  LYS   A CG   1 
ATOM   791  C  CD   A LYS   A 1 29  ? 14.735 0.695   21.324  0.70 32.51 ?  29  LYS   A CD   1 
ATOM   792  C  CD   B LYS   A 1 29  ? 15.241 1.428   21.378  0.30 28.79 ?  29  LYS   A CD   1 
ATOM   793  C  CE   A LYS   A 1 29  ? 13.863 0.037   22.382  0.70 34.14 ?  29  LYS   A CE   1 
ATOM   794  C  CE   B LYS   A 1 29  ? 14.443 1.033   22.602  0.30 29.85 ?  29  LYS   A CE   1 
ATOM   795  N  NZ   A LYS   A 1 29  ? 13.450 1.004   23.435  0.70 35.19 ?  29  LYS   A NZ   1 
ATOM   796  N  NZ   B LYS   A 1 29  ? 12.990 0.924   22.304  0.30 30.40 ?  29  LYS   A NZ   1 
ATOM   797  H  H    A LYS   A 1 29  ? 17.462 1.422   17.554  0.70 28.21 ?  29  LYS   A H    1 
ATOM   798  H  H    B LYS   A 1 29  ? 17.546 1.432   17.301  0.30 27.15 ?  29  LYS   A H    1 
ATOM   799  H  HA   A LYS   A 1 29  ? 17.211 1.423   20.200  0.70 30.10 ?  29  LYS   A HA   1 
ATOM   800  H  HA   B LYS   A 1 29  ? 17.401 1.781   19.955  0.30 29.14 ?  29  LYS   A HA   1 
ATOM   801  H  HB2  A LYS   A 1 29  ? 15.315 1.226   18.836  0.70 33.01 ?  29  LYS   A HB2  1 
ATOM   802  H  HB2  B LYS   A 1 29  ? 15.397 1.612   18.684  0.30 31.05 ?  29  LYS   A HB2  1 
ATOM   803  H  HB3  A LYS   A 1 29  ? 15.843 -0.177  18.316  0.70 33.01 ?  29  LYS   A HB3  1 
ATOM   804  H  HB3  B LYS   A 1 29  ? 15.766 0.100   18.374  0.30 31.05 ?  29  LYS   A HB3  1 
ATOM   805  H  HG2  A LYS   A 1 29  ? 14.230 -0.623  19.849  0.70 36.22 ?  29  LYS   A HG2  1 
ATOM   806  H  HG2  B LYS   A 1 29  ? 14.174 0.265   20.079  0.30 32.93 ?  29  LYS   A HG2  1 
ATOM   807  H  HG3  A LYS   A 1 29  ? 15.606 -0.989  20.557  0.70 36.22 ?  29  LYS   A HG3  1 
ATOM   808  H  HG3  B LYS   A 1 29  ? 15.498 -0.446  20.603  0.30 32.93 ?  29  LYS   A HG3  1 
ATOM   809  H  HD2  A LYS   A 1 29  ? 15.558 0.986   21.747  0.70 38.99 ?  29  LYS   A HD2  1 
ATOM   810  H  HD2  B LYS   A 1 29  ? 16.172 1.508   21.644  0.30 34.54 ?  29  LYS   A HD2  1 
ATOM   811  H  HD3  A LYS   A 1 29  ? 14.254 1.457   20.964  0.70 38.99 ?  29  LYS   A HD3  1 
ATOM   812  H  HD3  B LYS   A 1 29  ? 14.911 2.280   21.048  0.30 34.54 ?  29  LYS   A HD3  1 
ATOM   813  H  HE2  A LYS   A 1 29  ? 13.063 -0.316  21.962  0.70 40.95 ?  29  LYS   A HE2  1 
ATOM   814  H  HE2  B LYS   A 1 29  ? 14.757 0.172   22.921  0.30 35.81 ?  29  LYS   A HE2  1 
ATOM   815  H  HE3  A LYS   A 1 29  ? 14.362 -0.679  22.807  0.70 40.95 ?  29  LYS   A HE3  1 
ATOM   816  H  HE3  B LYS   A 1 29  ? 14.560 1.709   23.285  0.30 35.81 ?  29  LYS   A HE3  1 
ATOM   817  H  HZ1  A LYS   A 1 29  ? 12.941 0.595   24.041  0.70 42.22 ?  29  LYS   A HZ1  1 
ATOM   818  H  HZ1  B LYS   A 1 29  ? 12.540 0.757   23.053  0.30 36.47 ?  29  LYS   A HZ1  1 
ATOM   819  H  HZ2  A LYS   A 1 29  ? 14.168 1.339   23.839  0.70 42.22 ?  29  LYS   A HZ2  1 
ATOM   820  H  HZ2  B LYS   A 1 29  ? 12.695 1.686   21.952  0.30 36.47 ?  29  LYS   A HZ2  1 
ATOM   821  H  HZ3  A LYS   A 1 29  ? 12.985 1.670   23.070  0.70 42.22 ?  29  LYS   A HZ3  1 
ATOM   822  H  HZ3  B LYS   A 1 29  ? 12.846 0.263   21.726  0.30 36.47 ?  29  LYS   A HZ3  1 
ATOM   823  N  N    A VAL   A 1 30  ? 18.415 -1.220  18.824  0.70 23.53 ?  30  VAL   A N    1 
ATOM   824  N  N    B VAL   A 1 30  ? 18.355 -1.014  18.706  0.30 23.74 ?  30  VAL   A N    1 
ATOM   825  C  CA   A VAL   A 1 30  ? 19.078 -2.488  19.107  0.70 22.77 ?  30  VAL   A CA   1 
ATOM   826  C  CA   B VAL   A 1 30  ? 18.946 -2.303  19.049  0.30 23.36 ?  30  VAL   A CA   1 
ATOM   827  C  C    A VAL   A 1 30  ? 20.575 -2.304  19.331  0.70 21.56 ?  30  VAL   A C    1 
ATOM   828  C  C    B VAL   A 1 30  ? 20.444 -2.181  19.302  0.30 22.92 ?  30  VAL   A C    1 
ATOM   829  O  O    A VAL   A 1 30  ? 21.176 -3.019  20.140  0.70 22.05 ?  30  VAL   A O    1 
ATOM   830  O  O    B VAL   A 1 30  ? 20.991 -2.885  20.158  0.30 22.94 ?  30  VAL   A O    1 
ATOM   831  C  CB   A VAL   A 1 30  ? 18.793 -3.486  17.969  0.70 23.35 ?  30  VAL   A CB   1 
ATOM   832  C  CB   B VAL   A 1 30  ? 18.643 -3.330  17.944  0.30 23.41 ?  30  VAL   A CB   1 
ATOM   833  C  CG1  A VAL   A 1 30  ? 19.563 -4.786  18.179  0.70 23.69 ?  30  VAL   A CG1  1 
ATOM   834  C  CG1  B VAL   A 1 30  ? 19.361 -4.643  18.220  0.30 23.54 ?  30  VAL   A CG1  1 
ATOM   835  C  CG2  A VAL   A 1 30  ? 17.299 -3.756  17.860  0.70 23.75 ?  30  VAL   A CG2  1 
ATOM   836  C  CG2  B VAL   A 1 30  ? 17.142 -3.553  17.823  0.30 23.51 ?  30  VAL   A CG2  1 
ATOM   837  H  H    A VAL   A 1 30  ? 18.270 -1.076  17.990  0.70 28.22 ?  30  VAL   A H    1 
ATOM   838  H  H    B VAL   A 1 30  ? 18.218 -0.896  17.866  0.30 28.47 ?  30  VAL   A H    1 
ATOM   839  H  HA   A VAL   A 1 30  ? 18.700 -2.860  19.917  0.70 27.31 ?  30  VAL   A HA   1 
ATOM   840  H  HA   B VAL   A 1 30  ? 18.531 -2.624  19.864  0.30 28.02 ?  30  VAL   A HA   1 
ATOM   841  H  HB   A VAL   A 1 30  ? 19.086 -3.103  17.129  0.70 28.01 ?  30  VAL   A HB   1 
ATOM   842  H  HB   B VAL   A 1 30  ? 18.965 -2.989  17.094  0.30 28.07 ?  30  VAL   A HB   1 
ATOM   843  H  HG11 A VAL   A 1 30  ? 19.204 -5.464  17.583  0.70 28.42 ?  30  VAL   A HG11 1 
ATOM   844  H  HG11 B VAL   A 1 30  ? 18.977 -5.335  17.658  0.30 28.24 ?  30  VAL   A HG11 1 
ATOM   845  H  HG12 A VAL   A 1 30  ? 20.500 -4.637  17.980  0.70 28.42 ?  30  VAL   A HG12 1 
ATOM   846  H  HG12 B VAL   A 1 30  ? 20.304 -4.540  18.016  0.30 28.24 ?  30  VAL   A HG12 1 
ATOM   847  H  HG13 A VAL   A 1 30  ? 19.458 -5.070  19.100  0.70 28.42 ?  30  VAL   A HG13 1 
ATOM   848  H  HG13 B VAL   A 1 30  ? 19.245 -4.874  19.154  0.30 28.24 ?  30  VAL   A HG13 1 
ATOM   849  H  HG21 A VAL   A 1 30  ? 17.147 -4.427  17.175  0.70 28.49 ?  30  VAL   A HG21 1 
ATOM   850  H  HG21 B VAL   A 1 30  ? 16.975 -4.229  17.146  0.30 28.20 ?  30  VAL   A HG21 1 
ATOM   851  H  HG22 A VAL   A 1 30  ? 16.974 -4.079  18.715  0.70 28.49 ?  30  VAL   A HG22 1 
ATOM   852  H  HG22 B VAL   A 1 30  ? 16.799 -3.852  18.680  0.30 28.20 ?  30  VAL   A HG22 1 
ATOM   853  H  HG23 A VAL   A 1 30  ? 16.846 -2.933  17.623  0.70 28.49 ?  30  VAL   A HG23 1 
ATOM   854  H  HG23 B VAL   A 1 30  ? 16.719 -2.719  17.569  0.30 28.20 ?  30  VAL   A HG23 1 
ATOM   855  N  N    A LYS   A 1 31  ? 21.194 -1.351  18.641  0.70 20.57 ?  31  LYS   A N    1 
ATOM   856  N  N    B LYS   A 1 31  ? 21.122 -1.295  18.581  0.30 22.69 ?  31  LYS   A N    1 
ATOM   857  C  CA   A LYS   A 1 31  ? 22.645 -1.227  18.586  0.70 21.48 ?  31  LYS   A CA   1 
ATOM   858  C  CA   B LYS   A 1 31  ? 22.578 -1.225  18.567  0.30 22.96 ?  31  LYS   A CA   1 
ATOM   859  C  C    A LYS   A 1 31  ? 23.265 -2.584  18.243  0.70 19.55 ?  31  LYS   A C    1 
ATOM   860  C  C    B LYS   A 1 31  ? 23.177 -2.605  18.276  0.30 20.61 ?  31  LYS   A C    1 
ATOM   861  O  O    A LYS   A 1 31  ? 24.057 -3.127  19.021  0.70 20.55 ?  31  LYS   A O    1 
ATOM   862  O  O    B LYS   A 1 31  ? 23.869 -3.181  19.120  0.30 21.13 ?  31  LYS   A O    1 
ATOM   863  C  CB   A LYS   A 1 31  ? 23.220 -0.676  19.883  0.70 25.65 ?  31  LYS   A CB   1 
ATOM   864  C  CB   B LYS   A 1 31  ? 23.136 -0.646  19.859  0.30 25.81 ?  31  LYS   A CB   1 
ATOM   865  C  CG   A LYS   A 1 31  ? 22.542 0.589   20.377  0.70 30.33 ?  31  LYS   A CG   1 
ATOM   866  C  CG   B LYS   A 1 31  ? 22.459 0.641   20.303  0.30 28.76 ?  31  LYS   A CG   1 
ATOM   867  C  CD   A LYS   A 1 31  ? 23.561 1.630   20.816  0.70 33.85 ?  31  LYS   A CD   1 
ATOM   868  C  CD   B LYS   A 1 31  ? 23.466 1.623   20.880  0.30 31.11 ?  31  LYS   A CD   1 
ATOM   869  C  CE   A LYS   A 1 31  ? 22.935 2.670   21.729  0.70 36.08 ?  31  LYS   A CE   1 
ATOM   870  C  CE   B LYS   A 1 31  ? 22.788 2.687   21.728  0.30 32.60 ?  31  LYS   A CE   1 
ATOM   871  N  NZ   A LYS   A 1 31  ? 21.726 3.297   21.131  0.70 37.36 ?  31  LYS   A NZ   1 
ATOM   872  N  NZ   B LYS   A 1 31  ? 21.656 3.350   21.024  0.30 33.53 ?  31  LYS   A NZ   1 
ATOM   873  H  H    A LYS   A 1 31  ? 20.780 -0.751  18.187  0.70 24.67 ?  31  LYS   A H    1 
ATOM   874  H  H    B LYS   A 1 31  ? 20.745 -0.712  18.080  0.30 27.21 ?  31  LYS   A H    1 
ATOM   875  H  HA   A LYS   A 1 31  ? 22.870 -0.607  17.877  0.70 25.76 ?  31  LYS   A HA   1 
ATOM   876  H  HA   B LYS   A 1 31  ? 22.836 -0.628  17.853  0.30 27.54 ?  31  LYS   A HA   1 
ATOM   877  H  HB2  A LYS   A 1 31  ? 23.133 -1.349  20.572  0.70 30.77 ?  31  LYS   A HB2  1 
ATOM   878  H  HB2  B LYS   A 1 31  ? 23.024 -1.296  20.563  0.30 30.95 ?  31  LYS   A HB2  1 
ATOM   879  H  HB3  A LYS   A 1 31  ? 24.159 -0.471  19.741  0.70 30.77 ?  31  LYS   A HB3  1 
ATOM   880  H  HB3  B LYS   A 1 31  ? 24.080 -0.455  19.733  0.30 30.95 ?  31  LYS   A HB3  1 
ATOM   881  H  HG2  A LYS   A 1 31  ? 22.008 0.968   19.661  0.70 36.38 ?  31  LYS   A HG2  1 
ATOM   882  H  HG2  B LYS   A 1 31  ? 22.029 1.058   19.540  0.30 34.50 ?  31  LYS   A HG2  1 
ATOM   883  H  HG3  A LYS   A 1 31  ? 21.980 0.374   21.138  0.70 36.38 ?  31  LYS   A HG3  1 
ATOM   884  H  HG3  B LYS   A 1 31  ? 21.803 0.438   20.989  0.30 34.50 ?  31  LYS   A HG3  1 
ATOM   885  H  HD2  A LYS   A 1 31  ? 24.279 1.193   21.300  0.70 40.60 ?  31  LYS   A HD2  1 
ATOM   886  H  HD2  B LYS   A 1 31  ? 24.095 1.142   21.441  0.30 37.31 ?  31  LYS   A HD2  1 
ATOM   887  H  HD3  A LYS   A 1 31  ? 23.913 2.084   20.033  0.70 40.60 ?  31  LYS   A HD3  1 
ATOM   888  H  HD3  B LYS   A 1 31  ? 23.934 2.064   20.154  0.30 37.31 ?  31  LYS   A HD3  1 
ATOM   889  H  HE2  A LYS   A 1 31  ? 22.675 2.245   22.561  0.70 43.28 ?  31  LYS   A HE2  1 
ATOM   890  H  HE2  B LYS   A 1 31  ? 22.440 2.274   22.531  0.30 39.10 ?  31  LYS   A HE2  1 
ATOM   891  H  HE3  A LYS   A 1 31  ? 23.584 3.371   21.902  0.70 43.28 ?  31  LYS   A HE3  1 
ATOM   892  H  HE3  B LYS   A 1 31  ? 23.439 3.368   21.960  0.30 39.10 ?  31  LYS   A HE3  1 
ATOM   893  H  HZ1  A LYS   A 1 31  ? 21.406 3.923   21.677  0.70 44.82 ?  31  LYS   A HZ1  1 
ATOM   894  H  HZ1  B LYS   A 1 31  ? 21.313 3.991   21.538  0.30 40.22 ?  31  LYS   A HZ1  1 
ATOM   895  H  HZ2  A LYS   A 1 31  ? 21.931 3.672   20.351  0.70 44.82 ?  31  LYS   A HZ2  1 
ATOM   896  H  HZ2  B LYS   A 1 31  ? 21.941 3.711   20.263  0.30 40.22 ?  31  LYS   A HZ2  1 
ATOM   897  H  HZ3  A LYS   A 1 31  ? 21.097 2.681   20.999  0.70 44.82 ?  31  LYS   A HZ3  1 
ATOM   898  H  HZ3  B LYS   A 1 31  ? 21.020 2.755   20.843  0.30 40.22 ?  31  LYS   A HZ3  1 
ATOM   899  N  N    . PRO   A 1 32  ? 22.924 -3.153  17.091  1.00 18.10 ?  32  PRO   A N    1 
ATOM   900  C  CA   . PRO   A 1 32  ? 23.399 -4.499  16.772  1.00 17.55 ?  32  PRO   A CA   1 
ATOM   901  C  C    . PRO   A 1 32  ? 24.899 -4.521  16.557  1.00 17.56 ?  32  PRO   A C    1 
ATOM   902  O  O    . PRO   A 1 32  ? 25.549 -3.495  16.341  1.00 17.52 ?  32  PRO   A O    1 
ATOM   903  C  CB   . PRO   A 1 32  ? 22.668 -4.816  15.465  1.00 17.54 ?  32  PRO   A CB   1 
ATOM   904  C  CG   . PRO   A 1 32  ? 22.507 -3.473  14.816  1.00 16.43 ?  32  PRO   A CG   1 
ATOM   905  C  CD   . PRO   A 1 32  ? 22.221 -2.537  15.955  1.00 16.67 ?  32  PRO   A CD   1 
ATOM   906  H  HA   . PRO   A 1 32  ? 23.147 -5.131  17.461  1.00 21.04 ?  32  PRO   A HA   1 
ATOM   907  H  HB2  . PRO   A 1 32  ? 23.211 -5.407  14.915  1.00 21.04 ?  32  PRO   A HB2  1 
ATOM   908  H  HB3  . PRO   A 1 32  ? 21.805 -5.219  15.655  1.00 21.04 ?  32  PRO   A HB3  1 
ATOM   909  H  HG2  . PRO   A 1 32  ? 23.327 -3.236  14.358  1.00 19.70 ?  32  PRO   A HG2  1 
ATOM   910  H  HG3  . PRO   A 1 32  ? 21.761 -3.506  14.193  1.00 19.70 ?  32  PRO   A HG3  1 
ATOM   911  H  HD2  . PRO   A 1 32  ? 22.590 -1.661  15.748  1.00 19.99 ?  32  PRO   A HD2  1 
ATOM   912  H  HD3  . PRO   A 1 32  ? 21.271 -2.496  16.118  1.00 19.99 ?  32  PRO   A HD3  1 
ATOM   913  N  N    . THR   A 1 33  ? 25.445 -5.734  16.589  1.00 17.31 ?  33  THR   A N    1 
ATOM   914  C  CA   . THR   A 1 33  ? 26.857 -5.902  16.281  1.00 17.54 ?  33  THR   A CA   1 
ATOM   915  C  C    . THR   A 1 33  ? 27.163 -5.442  14.860  1.00 15.89 ?  33  THR   A C    1 
ATOM   916  O  O    . THR   A 1 33  ? 28.196 -4.800  14.617  1.00 16.36 ?  33  THR   A O    1 
ATOM   917  C  CB   . THR   A 1 33  ? 27.257 -7.363  16.479  1.00 19.56 ?  33  THR   A CB   1 
ATOM   918  O  OG1  . THR   A 1 33  ? 26.940 -7.762  17.816  1.00 21.31 ?  33  THR   A OG1  1 
ATOM   919  C  CG2  . THR   A 1 33  ? 28.746 -7.547  16.236  1.00 20.45 ?  33  THR   A CG2  1 
ATOM   920  H  H    . THR   A 1 33  ? 25.023 -6.460  16.771  1.00 20.76 ?  33  THR   A H    1 
ATOM   921  H  HA   . THR   A 1 33  ? 27.380 -5.362  16.893  1.00 21.03 ?  33  THR   A HA   1 
ATOM   922  H  HB   . THR   A 1 33  ? 26.770 -7.923  15.849  1.00 23.46 ?  33  THR   A HB   1 
ATOM   923  H  HG1  . THR   A 1 33  ? 27.363 -7.286  18.366  1.00 25.56 ?  33  THR   A HG1  1 
ATOM   924  H  HG21 . THR   A 1 33  ? 29.020 -8.432  16.523  1.00 24.52 ?  33  THR   A HG21 1 
ATOM   925  H  HG22 . THR   A 1 33  ? 28.946 -7.447  15.292  1.00 24.52 ?  33  THR   A HG22 1 
ATOM   926  H  HG23 . THR   A 1 33  ? 29.245 -6.885  16.738  1.00 24.52 ?  33  THR   A HG23 1 
ATOM   927  N  N    . VAL   A 1 34  ? 26.277 -5.756  13.914  1.00 14.30 ?  34  VAL   A N    1 
ATOM   928  C  CA   . VAL   A 1 34  ? 26.473 -5.430  12.505  1.00 13.11 ?  34  VAL   A CA   1 
ATOM   929  C  C    . VAL   A 1 34  ? 25.177 -4.869  11.935  1.00 12.45 ?  34  VAL   A C    1 
ATOM   930  O  O    . VAL   A 1 34  ? 24.135 -5.535  11.980  1.00 13.41 ?  34  VAL   A O    1 
ATOM   931  C  CB   . VAL   A 1 34  ? 26.915 -6.647  11.673  1.00 13.75 ?  34  VAL   A CB   1 
ATOM   932  C  CG1  . VAL   A 1 34  ? 27.108 -6.248  10.219  1.00 14.23 ?  34  VAL   A CG1  1 
ATOM   933  C  CG2  . VAL   A 1 34  ? 28.192 -7.274  12.247  1.00 15.07 ?  34  VAL   A CG2  1 
ATOM   934  H  H    . VAL   A 1 34  ? 25.543 -6.173  14.070  1.00 17.15 ?  34  VAL   A H    1 
ATOM   935  H  HA   . VAL   A 1 34  ? 27.157 -4.745  12.424  1.00 15.71 ?  34  VAL   A HA   1 
ATOM   936  H  HB   . VAL   A 1 34  ? 26.214 -7.317  11.711  1.00 16.48 ?  34  VAL   A HB   1 
ATOM   937  H  HG11 . VAL   A 1 34  ? 27.599 -6.952  9.766   1.00 17.06 ?  34  VAL   A HG11 1 
ATOM   938  H  HG12 . VAL   A 1 34  ? 26.241 -6.130  9.804   1.00 17.06 ?  34  VAL   A HG12 1 
ATOM   939  H  HG13 . VAL   A 1 34  ? 27.612 -5.421  10.185  1.00 17.06 ?  34  VAL   A HG13 1 
ATOM   940  H  HG21 . VAL   A 1 34  ? 28.460 -8.014  11.679  1.00 18.07 ?  34  VAL   A HG21 1 
ATOM   941  H  HG22 . VAL   A 1 34  ? 28.890 -6.604  12.271  1.00 18.07 ?  34  VAL   A HG22 1 
ATOM   942  H  HG23 . VAL   A 1 34  ? 28.011 -7.598  13.145  1.00 18.07 ?  34  VAL   A HG23 1 
ATOM   943  N  N    . VAL   A 1 35  ? 25.244 -3.660  11.381  1.00 11.79 ?  35  VAL   A N    1 
ATOM   944  C  CA   . VAL   A 1 35  ? 24.214 -3.145  10.488  1.00 11.54 ?  35  VAL   A CA   1 
ATOM   945  C  C    . VAL   A 1 35  ? 24.773 -3.153  9.072   1.00 10.93 ?  35  VAL   A C    1 
ATOM   946  O  O    . VAL   A 1 35  ? 25.921 -2.752  8.844   1.00 11.67 ?  35  VAL   A O    1 
ATOM   947  C  CB   . VAL   A 1 35  ? 23.686 -1.749  10.891  1.00 12.04 ?  35  VAL   A CB   1 
ATOM   948  C  CG1  . VAL   A 1 35  ? 24.757 -0.664  10.762  1.00 12.91 ?  35  VAL   A CG1  1 
ATOM   949  C  CG2  . VAL   A 1 35  ? 22.457 -1.395  10.057  1.00 12.78 ?  35  VAL   A CG2  1 
ATOM   950  H  H    . VAL   A 1 35  ? 25.893 -3.108  11.502  1.00 14.13 ?  35  VAL   A H    1 
ATOM   951  H  HA   . VAL   A 1 35  ? 23.457 -3.755  10.507  1.00 13.83 ?  35  VAL   A HA   1 
ATOM   952  H  HB   . VAL   A 1 35  ? 23.405 -1.779  11.817  1.00 14.43 ?  35  VAL   A HB   1 
ATOM   953  H  HG11 . VAL   A 1 35  ? 24.412 0.164   11.131  1.00 15.47 ?  35  VAL   A HG11 1 
ATOM   954  H  HG12 . VAL   A 1 35  ? 25.545 -0.943  11.251  1.00 15.47 ?  35  VAL   A HG12 1 
ATOM   955  H  HG13 . VAL   A 1 35  ? 24.974 -0.542  9.824   1.00 15.47 ?  35  VAL   A HG13 1 
ATOM   956  H  HG21 . VAL   A 1 35  ? 22.098 -0.552  10.364  1.00 15.32 ?  35  VAL   A HG21 1 
ATOM   957  H  HG22 . VAL   A 1 35  ? 22.719 -1.324  9.123   1.00 15.32 ?  35  VAL   A HG22 1 
ATOM   958  H  HG23 . VAL   A 1 35  ? 21.794 -2.098  10.158  1.00 15.32 ?  35  VAL   A HG23 1 
ATOM   959  N  N    . VAL   A 1 36  ? 23.960 -3.612  8.120   1.00 10.51 ?  36  VAL   A N    1 
ATOM   960  C  CA   . VAL   A 1 36  ? 24.337 -3.631  6.715   1.00 10.10 ?  36  VAL   A CA   1 
ATOM   961  C  C    . VAL   A 1 36  ? 23.876 -2.342  6.048   1.00 10.32 ?  36  VAL   A C    1 
ATOM   962  O  O    . VAL   A 1 36  ? 22.714 -1.935  6.178   1.00 11.06 ?  36  VAL   A O    1 
ATOM   963  C  CB   . VAL   A 1 36  ? 23.730 -4.846  6.003   1.00 10.25 ?  36  VAL   A CB   1 
ATOM   964  C  CG1  . VAL   A 1 36  ? 23.997 -4.781  4.518   1.00 10.99 ?  36  VAL   A CG1  1 
ATOM   965  C  CG2  . VAL   A 1 36  ? 24.275 -6.133  6.591   1.00 11.12 ?  36  VAL   A CG2  1 
ATOM   966  H  H    . VAL   A 1 36  ? 23.167 -3.924  8.269   1.00 12.60 ?  36  VAL   A H    1 
ATOM   967  H  HA   . VAL   A 1 36  ? 25.303 -3.693  6.641   1.00 12.10 ?  36  VAL   A HA   1 
ATOM   968  H  HB   . VAL   A 1 36  ? 22.767 -4.843  6.131   1.00 12.28 ?  36  VAL   A HB   1 
ATOM   969  H  HG11 . VAL   A 1 36  ? 23.858 -5.659  4.129   1.00 13.17 ?  36  VAL   A HG11 1 
ATOM   970  H  HG12 . VAL   A 1 36  ? 23.388 -4.144  4.108   1.00 13.17 ?  36  VAL   A HG12 1 
ATOM   971  H  HG13 . VAL   A 1 36  ? 24.915 -4.500  4.372   1.00 13.17 ?  36  VAL   A HG13 1 
ATOM   972  H  HG21 . VAL   A 1 36  ? 23.893 -6.890  6.115   1.00 13.32 ?  36  VAL   A HG21 1 
ATOM   973  H  HG22 . VAL   A 1 36  ? 25.241 -6.141  6.499   1.00 13.32 ?  36  VAL   A HG22 1 
ATOM   974  H  HG23 . VAL   A 1 36  ? 24.032 -6.182  7.530   1.00 13.32 ?  36  VAL   A HG23 1 
ATOM   975  N  N    . ASN   A 1 37  ? 24.800 -1.701  5.329   1.00 9.89  ?  37  ASN   A N    1 
ATOM   976  C  CA   . ASN   A 1 37  ? 24.475 -0.583  4.459   1.00 9.68  ?  37  ASN   A CA   1 
ATOM   977  C  C    . ASN   A 1 37  ? 24.344 -1.055  3.019   1.00 9.56  ?  37  ASN   A C    1 
ATOM   978  O  O    . ASN   A 1 37  ? 25.128 -1.890  2.547   1.00 10.52 ?  37  ASN   A O    1 
ATOM   979  C  CB   . ASN   A 1 37  ? 25.555 0.494   4.533   1.00 9.92  ?  37  ASN   A CB   1 
ATOM   980  C  CG   . ASN   A 1 37  ? 25.232 1.689   3.675   1.00 10.12 ?  37  ASN   A CG   1 
ATOM   981  O  OD1  . ASN   A 1 37  ? 24.062 2.024   3.480   1.00 10.92 ?  37  ASN   A OD1  1 
ATOM   982  N  ND2  . ASN   A 1 37  ? 26.269 2.345   3.161   1.00 10.43 ?  37  ASN   A ND2  1 
ATOM   983  H  H    . ASN   A 1 37  ? 25.637 -1.894  5.339   1.00 11.86 ?  37  ASN   A H    1 
ATOM   984  H  HA   . ASN   A 1 37  ? 23.634 -0.186  4.737   1.00 11.60 ?  37  ASN   A HA   1 
ATOM   985  H  HB2  . ASN   A 1 37  ? 25.644 0.794   5.454   1.00 11.89 ?  37  ASN   A HB2  1 
ATOM   986  H  HB3  . ASN   A 1 37  ? 26.399 0.118   4.228   1.00 11.89 ?  37  ASN   A HB3  1 
ATOM   987  H  HD21 . ASN   A 1 37  ? 26.135 3.034   2.662   1.00 12.50 ?  37  ASN   A HD21 1 
ATOM   988  H  HD22 . ASN   A 1 37  ? 27.067 2.086   3.317   1.00 12.50 ?  37  ASN   A HD22 1 
ATOM   989  N  N    A ALA   A 1 38  ? 23.329 -0.521  2.335   0.70 9.87  ?  38  ALA   A N    1 
ATOM   990  N  N    B ALA   A 1 38  ? 23.337 -0.522  2.323   0.30 9.81  ?  38  ALA   A N    1 
ATOM   991  C  CA   A ALA   A 1 38  ? 23.144 -0.681  0.895   0.70 10.40 ?  38  ALA   A CA   1 
ATOM   992  C  CA   B ALA   A 1 38  ? 23.173 -0.743  0.886   0.30 10.25 ?  38  ALA   A CA   1 
ATOM   993  C  C    A ALA   A 1 38  ? 24.053 0.321   0.182   0.70 10.32 ?  38  ALA   A C    1 
ATOM   994  C  C    B ALA   A 1 38  ? 24.040 0.275   0.148   0.30 10.18 ?  38  ALA   A C    1 
ATOM   995  O  O    A ALA   A 1 38  ? 23.640 1.411   -0.226  0.70 10.56 ?  38  ALA   A O    1 
ATOM   996  O  O    B ALA   A 1 38  ? 23.583 1.323   -0.319  0.30 10.21 ?  38  ALA   A O    1 
ATOM   997  C  CB   A ALA   A 1 38  ? 21.681 -0.462  0.531   0.70 11.32 ?  38  ALA   A CB   1 
ATOM   998  C  CB   B ALA   A 1 38  ? 21.707 -0.645  0.487   0.30 10.86 ?  38  ALA   A CB   1 
ATOM   999  H  H    A ALA   A 1 38  ? 22.723 -0.027  2.701   0.70 11.83 ?  38  ALA   A H    1 
ATOM   1000 H  H    B ALA   A 1 38  ? 22.729 -0.017  2.670   0.30 11.75 ?  38  ALA   A H    1 
ATOM   1001 H  HA   A ALA   A 1 38  ? 23.402 -1.577  0.633   0.70 12.46 ?  38  ALA   A HA   1 
ATOM   1002 H  HA   B ALA   A 1 38  ? 23.492 -1.630  0.664   0.30 12.29 ?  38  ALA   A HA   1 
ATOM   1003 H  HB1  A ALA   A 1 38  ? 21.571 -0.577  -0.425  0.70 13.56 ?  38  ALA   A HB1  1 
ATOM   1004 H  HB1  B ALA   A 1 38  ? 21.626 -0.838  -0.460  0.30 13.02 ?  38  ALA   A HB1  1 
ATOM   1005 H  HB2  A ALA   A 1 38  ? 21.136 -1.113  1.006   0.70 13.56 ?  38  ALA   A HB2  1 
ATOM   1006 H  HB2  B ALA   A 1 38  ? 21.195 -1.289  1.001   0.30 13.02 ?  38  ALA   A HB2  1 
ATOM   1007 H  HB3  A ALA   A 1 38  ? 21.419 0.436   0.789   0.70 13.56 ?  38  ALA   A HB3  1 
ATOM   1008 H  HB3  B ALA   A 1 38  ? 21.390 0.252   0.669   0.30 13.02 ?  38  ALA   A HB3  1 
ATOM   1009 N  N    . ALA   A 1 39  ? 25.320 -0.056  0.043   1.00 10.35 ?  39  ALA   A N    1 
ATOM   1010 C  CA   . ALA   A 1 39  ? 26.349 0.838   -0.458  1.00 10.40 ?  39  ALA   A CA   1 
ATOM   1011 C  C    . ALA   A 1 39  ? 26.479 0.776   -1.975  1.00 10.23 ?  39  ALA   A C    1 
ATOM   1012 O  O    . ALA   A 1 39  ? 26.007 -0.153  -2.634  1.00 10.75 ?  39  ALA   A O    1 
ATOM   1013 C  CB   . ALA   A 1 39  ? 27.689 0.468   0.185   1.00 11.59 ?  39  ALA   A CB   1 
ATOM   1014 H  H    A ALA   A 1 39  ? 25.610 -0.843  0.241   0.70 12.41 ?  39  ALA   A H    1 
ATOM   1015 H  H    B ALA   A 1 39  ? 25.625 -0.831  0.266   0.30 12.41 ?  39  ALA   A H    1 
ATOM   1016 H  HA   . ALA   A 1 39  ? 26.124 1.751   -0.206  1.00 12.46 ?  39  ALA   A HA   1 
ATOM   1017 H  HB1  . ALA   A 1 39  ? 28.369 1.075   -0.149  1.00 13.90 ?  39  ALA   A HB1  1 
ATOM   1018 H  HB2  . ALA   A 1 39  ? 27.609 0.565   1.150   1.00 13.90 ?  39  ALA   A HB2  1 
ATOM   1019 H  HB3  . ALA   A 1 39  ? 27.906 -0.441  -0.043  1.00 13.90 ?  39  ALA   A HB3  1 
ATOM   1020 N  N    A ASN   A 1 40  ? 27.187 1.770   -2.519  0.70 10.77 ?  40  ASN   A N    1 
ATOM   1021 N  N    B ASN   A 1 40  ? 27.076 1.819   -2.539  0.30 10.26 ?  40  ASN   A N    1 
ATOM   1022 C  CA   A ASN   A 1 40  ? 27.751 1.715   -3.861  0.70 10.59 ?  40  ASN   A CA   1 
ATOM   1023 C  CA   B ASN   A 1 40  ? 27.528 1.789   -3.921  0.30 10.36 ?  40  ASN   A CA   1 
ATOM   1024 C  C    A ASN   A 1 40  ? 29.273 1.603   -3.774  0.70 10.19 ?  40  ASN   A C    1 
ATOM   1025 C  C    B ASN   A 1 40  ? 29.048 1.663   -3.933  0.30 9.86  ?  40  ASN   A C    1 
ATOM   1026 O  O    A ASN   A 1 40  ? 29.863 1.711   -2.695  0.70 10.37 ?  40  ASN   A O    1 
ATOM   1027 O  O    B ASN   A 1 40  ? 29.706 1.740   -2.893  0.30 10.16 ?  40  ASN   A O    1 
ATOM   1028 C  CB   A ASN   A 1 40  ? 27.279 2.890   -4.739  0.70 11.39 ?  40  ASN   A CB   1 
ATOM   1029 C  CB   B ASN   A 1 40  ? 27.052 3.026   -4.696  0.30 11.16 ?  40  ASN   A CB   1 
ATOM   1030 C  CG   A ASN   A 1 40  ? 27.631 4.248   -4.167  0.70 11.93 ?  40  ASN   A CG   1 
ATOM   1031 C  CG   B ASN   A 1 40  ? 27.480 4.322   -4.050  0.30 12.06 ?  40  ASN   A CG   1 
ATOM   1032 O  OD1  A ASN   A 1 40  ? 28.789 4.506   -3.824  0.70 12.83 ?  40  ASN   A OD1  1 
ATOM   1033 O  OD1  B ASN   A 1 40  ? 28.671 4.631   -3.980  0.30 12.47 ?  40  ASN   A OD1  1 
ATOM   1034 N  ND2  A ASN   A 1 40  ? 26.628 5.135   -4.071  0.70 12.08 ?  40  ASN   A ND2  1 
ATOM   1035 N  ND2  B ASN   A 1 40  ? 26.506 5.098   -3.583  0.30 12.45 ?  40  ASN   A ND2  1 
ATOM   1036 H  H    A ASN   A 1 40  ? 27.370 2.500   -2.107  0.70 12.91 ?  40  ASN   A H    1 
ATOM   1037 H  H    B ASN   A 1 40  ? 27.227 2.564   -2.137  0.30 12.30 ?  40  ASN   A H    1 
ATOM   1038 H  HA   A ASN   A 1 40  ? 27.443 0.903   -4.286  0.70 12.69 ?  40  ASN   A HA   1 
ATOM   1039 H  HA   B ASN   A 1 40  ? 27.151 1.003   -4.359  0.30 12.41 ?  40  ASN   A HA   1 
ATOM   1040 H  HB2  A ASN   A 1 40  ? 27.696 2.816   -5.614  0.70 13.65 ?  40  ASN   A HB2  1 
ATOM   1041 H  HB2  B ASN   A 1 40  ? 27.425 2.997   -5.591  0.30 13.37 ?  40  ASN   A HB2  1 
ATOM   1042 H  HB3  A ASN   A 1 40  ? 26.316 2.844   -4.828  0.70 13.65 ?  40  ASN   A HB3  1 
ATOM   1043 H  HB3  B ASN   A 1 40  ? 26.080 3.017   -4.744  0.30 13.37 ?  40  ASN   A HB3  1 
ATOM   1044 H  HD21 A ASN   A 1 40  ? 26.773 5.925   -3.755  0.70 14.48 ?  40  ASN   A HD21 1 
ATOM   1045 H  HD21 B ASN   A 1 40  ? 26.697 5.846   -3.206  0.30 14.92 ?  40  ASN   A HD21 1 
ATOM   1046 H  HD22 A ASN   A 1 40  ? 25.833 4.915   -4.316  0.70 14.48 ?  40  ASN   A HD22 1 
ATOM   1047 H  HD22 B ASN   A 1 40  ? 25.684 4.851   -3.657  0.30 14.92 ?  40  ASN   A HD22 1 
ATOM   1048 N  N    A VAL   A 1 41  ? 29.908 1.342   -4.922  0.70 10.53 ?  41  VAL   A N    1 
ATOM   1049 N  N    B VAL   A 1 41  ? 29.610 1.452   -5.125  0.30 9.87  ?  41  VAL   A N    1 
ATOM   1050 C  CA   A VAL   A 1 41  ? 31.339 1.037   -4.937  0.70 11.21 ?  41  VAL   A CA   1 
ATOM   1051 C  CA   B VAL   A 1 41  ? 31.031 1.123   -5.210  0.30 10.24 ?  41  VAL   A CA   1 
ATOM   1052 C  C    A VAL   A 1 41  ? 32.186 2.199   -4.455  0.70 11.12 ?  41  VAL   A C    1 
ATOM   1053 C  C    B VAL   A 1 41  ? 31.932 2.245   -4.706  0.30 10.38 ?  41  VAL   A C    1 
ATOM   1054 O  O    A VAL   A 1 41  ? 33.311 1.988   -3.987  0.70 11.41 ?  41  VAL   A O    1 
ATOM   1055 O  O    B VAL   A 1 41  ? 33.096 1.992   -4.373  0.30 10.06 ?  41  VAL   A O    1 
ATOM   1056 C  CB   A VAL   A 1 41  ? 31.838 0.542   -6.318  0.70 11.33 ?  41  VAL   A CB   1 
ATOM   1057 C  CB   B VAL   A 1 41  ? 31.439 0.701   -6.637  0.30 11.03 ?  41  VAL   A CB   1 
ATOM   1058 C  CG1  A VAL   A 1 41  ? 31.146 -0.752  -6.719  0.70 12.16 ?  41  VAL   A CG1  1 
ATOM   1059 C  CG1  B VAL   A 1 41  ? 30.812 -0.639  -7.001  0.30 11.46 ?  41  VAL   A CG1  1 
ATOM   1060 C  CG2  A VAL   A 1 41  ? 31.695 1.614   -7.403  0.70 11.31 ?  41  VAL   A CG2  1 
ATOM   1061 C  CG2  B VAL   A 1 41  ? 31.072 1.781   -7.645  0.30 11.45 ?  41  VAL   A CG2  1 
ATOM   1062 H  H    A VAL   A 1 41  ? 29.542 1.332   -5.695  0.70 12.62 ?  41  VAL   A H    1 
ATOM   1063 H  H    B VAL   A 1 41  ? 29.194 1.489   -5.878  0.30 11.83 ?  41  VAL   A H    1 
ATOM   1064 H  HA   A VAL   A 1 41  ? 31.505 0.314   -4.317  0.70 13.44 ?  41  VAL   A HA   1 
ATOM   1065 H  HA   B VAL   A 1 41  ? 31.182 0.352   -4.639  0.30 12.27 ?  41  VAL   A HA   1 
ATOM   1066 H  HB   A VAL   A 1 41  ? 32.786 0.343   -6.250  0.70 13.58 ?  41  VAL   A HB   1 
ATOM   1067 H  HB   B VAL   A 1 41  ? 32.401 0.590   -6.658  0.30 13.22 ?  41  VAL   A HB   1 
ATOM   1068 H  HG11 A VAL   A 1 41  ? 31.486 -1.049  -7.578  0.70 14.57 ?  41  VAL   A HG11 1 
ATOM   1069 H  HG11 B VAL   A 1 41  ? 31.068 -0.871  -7.906  0.30 13.74 ?  41  VAL   A HG11 1 
ATOM   1070 H  HG12 A VAL   A 1 41  ? 31.319 -1.427  -6.044  0.70 14.57 ?  41  VAL   A HG12 1 
ATOM   1071 H  HG12 B VAL   A 1 41  ? 31.134 -1.317  -6.383  0.30 13.74 ?  41  VAL   A HG12 1 
ATOM   1072 H  HG13 A VAL   A 1 41  ? 30.188 -0.593  -6.783  0.70 14.57 ?  41  VAL   A HG13 1 
ATOM   1073 H  HG13 B VAL   A 1 41  ? 29.848 -0.569  -6.936  0.30 13.74 ?  41  VAL   A HG13 1 
ATOM   1074 H  HG21 A VAL   A 1 41  ? 31.923 1.226   -8.266  0.70 13.56 ?  41  VAL   A HG21 1 
ATOM   1075 H  HG21 B VAL   A 1 41  ? 31.433 1.535   -8.510  0.30 13.72 ?  41  VAL   A HG21 1 
ATOM   1076 H  HG22 A VAL   A 1 41  ? 30.783 1.933   -7.415  0.70 13.56 ?  41  VAL   A HG22 1 
ATOM   1077 H  HG22 B VAL   A 1 41  ? 30.106 1.851   -7.699  0.30 13.72 ?  41  VAL   A HG22 1 
ATOM   1078 H  HG23 A VAL   A 1 41  ? 32.303 2.346   -7.207  0.70 13.56 ?  41  VAL   A HG23 1 
ATOM   1079 H  HG23 B VAL   A 1 41  ? 31.450 2.625   -7.356  0.30 13.72 ?  41  VAL   A HG23 1 
ATOM   1080 N  N    A TYR   A 1 42  ? 31.682 3.428   -4.577  0.70 11.39 ?  42  TYR   A N    1 
ATOM   1081 N  N    B TYR   A 1 42  ? 31.441 3.487   -4.668  0.30 10.66 ?  42  TYR   A N    1 
ATOM   1082 C  CA   A TYR   A 1 42  ? 32.398 4.629   -4.162  0.70 11.63 ?  42  TYR   A CA   1 
ATOM   1083 C  CA   B TYR   A 1 42  ? 32.249 4.628   -4.243  0.30 11.16 ?  42  TYR   A CA   1 
ATOM   1084 C  C    A TYR   A 1 42  ? 32.115 5.003   -2.717  0.70 10.94 ?  42  TYR   A C    1 
ATOM   1085 C  C    B TYR   A 1 42  ? 32.038 5.014   -2.784  0.30 10.92 ?  42  TYR   A C    1 
ATOM   1086 O  O    A TYR   A 1 42  ? 32.681 5.989   -2.219  0.70 11.52 ?  42  TYR   A O    1 
ATOM   1087 O  O    B TYR   A 1 42  ? 32.605 6.018   -2.335  0.30 11.19 ?  42  TYR   A O    1 
ATOM   1088 C  CB   A TYR   A 1 42  ? 32.040 5.808   -5.089  0.70 12.08 ?  42  TYR   A CB   1 
ATOM   1089 C  CB   B TYR   A 1 42  ? 31.954 5.844   -5.124  0.30 11.70 ?  42  TYR   A CB   1 
ATOM   1090 C  CG   A TYR   A 1 42  ? 32.248 5.487   -6.553  0.70 12.53 ?  42  TYR   A CG   1 
ATOM   1091 C  CG   B TYR   A 1 42  ? 32.080 5.564   -6.599  0.30 12.19 ?  42  TYR   A CG   1 
ATOM   1092 C  CD1  A TYR   A 1 42  ? 33.520 5.288   -7.063  0.70 13.38 ?  42  TYR   A CD1  1 
ATOM   1093 C  CD1  B TYR   A 1 42  ? 33.320 5.344   -7.181  0.30 12.46 ?  42  TYR   A CD1  1 
ATOM   1094 C  CD2  A TYR   A 1 42  ? 31.169 5.344   -7.417  0.70 13.80 ?  42  TYR   A CD2  1 
ATOM   1095 C  CD2  B TYR   A 1 42  ? 30.957 5.515   -7.410  0.30 13.07 ?  42  TYR   A CD2  1 
ATOM   1096 C  CE1  A TYR   A 1 42  ? 33.717 4.971   -8.395  0.70 13.92 ?  42  TYR   A CE1  1 
ATOM   1097 C  CE1  B TYR   A 1 42  ? 33.437 5.082   -8.532  0.30 12.75 ?  42  TYR   A CE1  1 
ATOM   1098 C  CE2  A TYR   A 1 42  ? 31.360 5.035   -8.754  0.70 14.67 ?  42  TYR   A CE2  1 
ATOM   1099 C  CE2  B TYR   A 1 42  ? 31.064 5.260   -8.759  0.30 13.39 ?  42  TYR   A CE2  1 
ATOM   1100 C  CZ   A TYR   A 1 42  ? 32.638 4.847   -9.236  0.70 14.49 ?  42  TYR   A CZ   1 
ATOM   1101 C  CZ   B TYR   A 1 42  ? 32.304 5.042   -9.317  0.30 13.29 ?  42  TYR   A CZ   1 
ATOM   1102 O  OH   A TYR   A 1 42  ? 32.837 4.530   -10.560 0.70 15.58 ?  42  TYR   A OH   1 
ATOM   1103 O  OH   B TYR   A 1 42  ? 32.409 4.787   -10.664 0.30 13.74 ?  42  TYR   A OH   1 
ATOM   1104 H  H    A TYR   A 1 42  ? 30.906 3.593   -4.905  0.70 13.65 ?  42  TYR   A H    1 
ATOM   1105 H  H    B TYR   A 1 42  ? 30.636 3.696   -4.911  0.30 12.77 ?  42  TYR   A H    1 
ATOM   1106 H  HA   A TYR   A 1 42  ? 33.351 4.477   -4.244  0.70 13.94 ?  42  TYR   A HA   1 
ATOM   1107 H  HA   B TYR   A 1 42  ? 33.181 4.399   -4.362  0.30 13.38 ?  42  TYR   A HA   1 
ATOM   1108 H  HB2  A TYR   A 1 42  ? 31.104 6.039   -4.963  0.70 14.48 ?  42  TYR   A HB2  1 
ATOM   1109 H  HB2  B TYR   A 1 42  ? 31.047 6.144   -4.951  0.30 14.02 ?  42  TYR   A HB2  1 
ATOM   1110 H  HB3  A TYR   A 1 42  ? 32.599 6.570   -4.869  0.70 14.48 ?  42  TYR   A HB3  1 
ATOM   1111 H  HB3  B TYR   A 1 42  ? 32.582 6.549   -4.898  0.30 14.02 ?  42  TYR   A HB3  1 
ATOM   1112 H  HD1  A TYR   A 1 42  ? 34.256 5.367   -6.500  0.70 16.04 ?  42  TYR   A HD1  1 
ATOM   1113 H  HD1  B TYR   A 1 42  ? 34.084 5.368   -6.649  0.30 14.93 ?  42  TYR   A HD1  1 
ATOM   1114 H  HD2  A TYR   A 1 42  ? 30.305 5.473   -7.095  0.70 16.54 ?  42  TYR   A HD2  1 
ATOM   1115 H  HD2  B TYR   A 1 42  ? 30.118 5.661   -7.035  0.30 15.67 ?  42  TYR   A HD2  1 
ATOM   1116 H  HE1  A TYR   A 1 42  ? 34.578 4.847   -8.723  0.70 16.68 ?  42  TYR   A HE1  1 
ATOM   1117 H  HE1  B TYR   A 1 42  ? 34.276 4.936   -8.907  0.30 15.29 ?  42  TYR   A HE1  1 
ATOM   1118 H  HE2  A TYR   A 1 42  ? 30.625 4.952   -9.324  0.70 17.58 ?  42  TYR   A HE2  1 
ATOM   1119 H  HE2  B TYR   A 1 42  ? 30.303 5.230   -9.290  0.30 16.05 ?  42  TYR   A HE2  1 
ATOM   1120 H  HH   A TYR   A 1 42  ? 33.657 4.430   -10.712 0.70 18.69 ?  42  TYR   A HH   1 
ATOM   1121 H  HH   B TYR   A 1 42  ? 31.650 4.791   -11.017 0.30 16.48 ?  42  TYR   A HH   1 
ATOM   1122 N  N    . LEU   A 1 43  ? 31.237 4.247   -2.047  1.00 10.80 ?  43  LEU   A N    1 
ATOM   1123 C  CA   . LEU   A 1 43  ? 30.798 4.590   -0.697  1.00 10.56 ?  43  LEU   A CA   1 
ATOM   1124 C  C    . LEU   A 1 43  ? 30.316 6.038   -0.610  1.00 10.64 ?  43  LEU   A C    1 
ATOM   1125 O  O    . LEU   A 1 43  ? 30.579 6.744   0.363   1.00 11.63 ?  43  LEU   A O    1 
ATOM   1126 C  CB   . LEU   A 1 43  ? 31.843 4.282   0.369   1.00 11.14 ?  43  LEU   A CB   1 
ATOM   1127 C  CG   . LEU   A 1 43  ? 32.338 2.834   0.465   1.00 11.25 ?  43  LEU   A CG   1 
ATOM   1128 C  CD1  . LEU   A 1 43  ? 33.373 2.720   1.575   1.00 12.29 ?  43  LEU   A CD1  1 
ATOM   1129 C  CD2  . LEU   A 1 43  ? 31.195 1.855   0.697   1.00 11.90 ?  43  LEU   A CD2  1 
ATOM   1130 H  H    A LEU   A 1 43  ? 30.882 3.519   -2.351  0.70 12.94 ?  43  LEU   A H    1 
ATOM   1131 H  H    B LEU   A 1 43  ? 30.913 3.492   -2.319  0.30 12.94 ?  43  LEU   A H    1 
ATOM   1132 H  HA   . LEU   A 1 43  ? 30.028 4.033   -0.489  1.00 12.66 ?  43  LEU   A HA   1 
ATOM   1133 H  HB2  . LEU   A 1 43  ? 32.617 4.844   0.203   1.00 13.35 ?  43  LEU   A HB2  1 
ATOM   1134 H  HB3  . LEU   A 1 43  ? 31.465 4.513   1.235   1.00 13.35 ?  43  LEU   A HB3  1 
ATOM   1135 H  HG   . LEU   A 1 43  ? 32.777 2.593   -0.366  1.00 13.48 ?  43  LEU   A HG   1 
ATOM   1136 H  HD11 . LEU   A 1 43  ? 33.680 1.801   1.629   1.00 14.73 ?  43  LEU   A HD11 1 
ATOM   1137 H  HD12 . LEU   A 1 43  ? 34.117 3.308   1.377   1.00 14.73 ?  43  LEU   A HD12 1 
ATOM   1138 H  HD13 . LEU   A 1 43  ? 32.961 2.978   2.416   1.00 14.73 ?  43  LEU   A HD13 1 
ATOM   1139 H  HD21 . LEU   A 1 43  ? 31.565 0.970   0.845   1.00 14.27 ?  43  LEU   A HD21 1 
ATOM   1140 H  HD22 . LEU   A 1 43  ? 30.693 2.140   1.473   1.00 14.27 ?  43  LEU   A HD22 1 
ATOM   1141 H  HD23 . LEU   A 1 43  ? 30.627 1.850   -0.087  1.00 14.27 ?  43  LEU   A HD23 1 
ATOM   1142 N  N    A LYS   A 1 44  ? 29.589 6.479   -1.637  0.70 11.05 ?  44  LYS   A N    1 
ATOM   1143 N  N    B LYS   A 1 44  ? 29.593 6.474   -1.643  0.30 11.22 ?  44  LYS   A N    1 
ATOM   1144 C  CA   A LYS   A 1 44  ? 28.952 7.795   -1.631  0.70 11.25 ?  44  LYS   A CA   1 
ATOM   1145 C  CA   B LYS   A 1 44  ? 28.933 7.780   -1.658  0.30 11.81 ?  44  LYS   A CA   1 
ATOM   1146 C  C    A LYS   A 1 44  ? 27.521 7.614   -1.144  0.70 10.51 ?  44  LYS   A C    1 
ATOM   1147 C  C    B LYS   A 1 44  ? 27.519 7.571   -1.132  0.30 10.95 ?  44  LYS   A C    1 
ATOM   1148 O  O    A LYS   A 1 44  ? 26.653 7.124   -1.874  0.70 11.58 ?  44  LYS   A O    1 
ATOM   1149 O  O    B LYS   A 1 44  ? 26.656 7.026   -1.826  0.30 11.19 ?  44  LYS   A O    1 
ATOM   1150 C  CB   A LYS   A 1 44  ? 29.009 8.431   -3.012  0.70 13.37 ?  44  LYS   A CB   1 
ATOM   1151 C  CB   B LYS   A 1 44  ? 28.916 8.357   -3.069  0.30 13.74 ?  44  LYS   A CB   1 
ATOM   1152 C  CG   A LYS   A 1 44  ? 30.401 8.875   -3.428  0.70 16.53 ?  44  LYS   A CG   1 
ATOM   1153 C  CG   B LYS   A 1 44  ? 30.250 8.905   -3.543  0.30 16.20 ?  44  LYS   A CG   1 
ATOM   1154 C  CD   A LYS   A 1 44  ? 31.068 9.764   -2.383  0.70 21.42 ?  44  LYS   A CD   1 
ATOM   1155 C  CD   B LYS   A 1 44  ? 30.830 9.904   -2.554  0.30 18.95 ?  44  LYS   A CD   1 
ATOM   1156 C  CE   A LYS   A 1 44  ? 32.402 10.289  -2.880  0.70 24.29 ?  44  LYS   A CE   1 
ATOM   1157 C  CE   B LYS   A 1 44  ? 32.044 10.599  -3.136  0.30 20.77 ?  44  LYS   A CE   1 
ATOM   1158 N  NZ   A LYS   A 1 44  ? 33.207 10.884  -1.781  0.70 25.82 ?  44  LYS   A NZ   1 
ATOM   1159 N  NZ   B LYS   A 1 44  ? 33.016 11.004  -2.087  0.30 22.04 ?  44  LYS   A NZ   1 
ATOM   1160 H  H    A LYS   A 1 44  ? 29.450 6.027   -2.357  0.70 13.24 ?  44  LYS   A H    1 
ATOM   1161 H  H    B LYS   A 1 44  ? 29.462 6.019   -2.361  0.30 13.44 ?  44  LYS   A H    1 
ATOM   1162 H  HA   A LYS   A 1 44  ? 29.401 8.365   -0.992  0.70 13.48 ?  44  LYS   A HA   1 
ATOM   1163 H  HA   B LYS   A 1 44  ? 29.391 8.390   -1.060  0.30 14.15 ?  44  LYS   A HA   1 
ATOM   1164 H  HB2  A LYS   A 1 44  ? 28.696 7.789   -3.666  0.70 16.02 ?  44  LYS   A HB2  1 
ATOM   1165 H  HB2  B LYS   A 1 44  ? 28.653 7.658   -3.689  0.30 16.47 ?  44  LYS   A HB2  1 
ATOM   1166 H  HB3  A LYS   A 1 44  ? 28.436 9.214   -3.016  0.70 16.02 ?  44  LYS   A HB3  1 
ATOM   1167 H  HB3  B LYS   A 1 44  ? 28.275 9.083   -3.104  0.30 16.47 ?  44  LYS   A HB3  1 
ATOM   1168 H  HG2  A LYS   A 1 44  ? 30.961 8.094   -3.558  0.70 19.83 ?  44  LYS   A HG2  1 
ATOM   1169 H  HG2  B LYS   A 1 44  ? 30.881 8.174   -3.643  0.30 19.42 ?  44  LYS   A HG2  1 
ATOM   1170 H  HG3  A LYS   A 1 44  ? 30.341 9.382   -4.255  0.70 19.83 ?  44  LYS   A HG3  1 
ATOM   1171 H  HG3  B LYS   A 1 44  ? 30.128 9.359   -4.393  0.30 19.42 ?  44  LYS   A HG3  1 
ATOM   1172 H  HD2  A LYS   A 1 44  ? 30.487 10.517  -2.185  0.70 25.69 ?  44  LYS   A HD2  1 
ATOM   1173 H  HD2  B LYS   A 1 44  ? 30.157 10.569  -2.338  0.30 22.73 ?  44  LYS   A HD2  1 
ATOM   1174 H  HD3  A LYS   A 1 44  ? 31.235 9.246   -1.579  0.70 25.69 ?  44  LYS   A HD3  1 
ATOM   1175 H  HD3  B LYS   A 1 44  ? 31.110 9.434   -1.751  0.30 22.73 ?  44  LYS   A HD3  1 
ATOM   1176 H  HE2  A LYS   A 1 44  ? 32.908 9.556   -3.263  0.70 29.13 ?  44  LYS   A HE2  1 
ATOM   1177 H  HE2  B LYS   A 1 44  ? 32.492 9.993   -3.747  0.30 24.91 ?  44  LYS   A HE2  1 
ATOM   1178 H  HE3  A LYS   A 1 44  ? 32.244 10.973  -3.548  0.70 29.13 ?  44  LYS   A HE3  1 
ATOM   1179 H  HE3  B LYS   A 1 44  ? 31.755 11.395  -3.605  0.30 24.91 ?  44  LYS   A HE3  1 
ATOM   1180 H  HZ1  A LYS   A 1 44  ? 33.980 11.185  -2.102  0.70 30.97 ?  44  LYS   A HZ1  1 
ATOM   1181 H  HZ1  B LYS   A 1 44  ? 33.715 11.408  -2.462  0.30 26.43 ?  44  LYS   A HZ1  1 
ATOM   1182 H  HZ2  A LYS   A 1 44  ? 32.762 11.565  -1.415  0.70 30.97 ?  44  LYS   A HZ2  1 
ATOM   1183 H  HZ2  B LYS   A 1 44  ? 32.630 11.564  -1.514  0.30 26.43 ?  44  LYS   A HZ2  1 
ATOM   1184 H  HZ3  A LYS   A 1 44  ? 33.367 10.275  -1.156  0.70 30.97 ?  44  LYS   A HZ3  1 
ATOM   1185 H  HZ3  B LYS   A 1 44  ? 33.301 10.286  -1.643  0.30 26.43 ?  44  LYS   A HZ3  1 
ATOM   1186 N  N    . HIS   A 1 45  ? 27.283 7.989   0.108   1.00 10.57 ?  45  HIS   A N    1 
ATOM   1187 C  CA   . HIS   A 1 45  ? 26.042 7.654   0.801   1.00 10.55 ?  45  HIS   A CA   1 
ATOM   1188 C  C    . HIS   A 1 45  ? 25.028 8.785   0.635   1.00 11.32 ?  45  HIS   A C    1 
ATOM   1189 O  O    . HIS   A 1 45  ? 24.746 9.553   1.552   1.00 13.27 ?  45  HIS   A O    1 
ATOM   1190 C  CB   . HIS   A 1 45  ? 26.334 7.396   2.267   1.00 10.76 ?  45  HIS   A CB   1 
ATOM   1191 C  CG   . HIS   A 1 45  ? 27.452 6.435   2.496   1.00 10.13 ?  45  HIS   A CG   1 
ATOM   1192 N  ND1  . HIS   A 1 45  ? 27.446 5.146   2.004   1.00 10.54 ?  45  HIS   A ND1  1 
ATOM   1193 C  CD2  . HIS   A 1 45  ? 28.617 6.589   3.171   1.00 10.31 ?  45  HIS   A CD2  1 
ATOM   1194 C  CE1  . HIS   A 1 45  ? 28.562 4.547   2.384   1.00 10.58 ?  45  HIS   A CE1  1 
ATOM   1195 N  NE2  . HIS   A 1 45  ? 29.292 5.401   3.083   1.00 10.66 ?  45  HIS   A NE2  1 
ATOM   1196 H  H    A HIS   A 1 45  ? 27.831 8.451   0.583   0.70 12.67 ?  45  HIS   A H    1 
ATOM   1197 H  H    B HIS   A 1 45  ? 27.832 8.454   0.578   0.30 12.67 ?  45  HIS   A H    1 
ATOM   1198 H  HA   . HIS   A 1 45  ? 25.661 6.846   0.416   1.00 12.65 ?  45  HIS   A HA   1 
ATOM   1199 H  HB2  . HIS   A 1 45  ? 26.562 8.234   2.694   1.00 12.89 ?  45  HIS   A HB2  1 
ATOM   1200 H  HB3  . HIS   A 1 45  ? 25.533 7.026   2.685   1.00 12.89 ?  45  HIS   A HB3  1 
ATOM   1201 H  HD2  . HIS   A 1 45  ? 28.909 7.364   3.604   1.00 12.35 ?  45  HIS   A HD2  1 
ATOM   1202 H  HE1  . HIS   A 1 45  ? 28.800 3.671   2.191   1.00 12.68 ?  45  HIS   A HE1  1 
ATOM   1203 H  HE2  . HIS   A 1 45  ? 30.065 5.240   3.428   1.00 12.77 ?  45  HIS   A HE2  1 
ATOM   1204 N  N    A GLY   A 1 46  ? 24.427 8.839   -0.548  0.70 12.07 ?  46  GLY   A N    1 
ATOM   1205 N  N    B GLY   A 1 46  ? 24.490 8.893   -0.576  0.30 11.57 ?  46  GLY   A N    1 
ATOM   1206 C  CA   A GLY   A 1 46  ? 23.585 9.968   -0.892  0.70 12.73 ?  46  GLY   A CA   1 
ATOM   1207 C  CA   B GLY   A 1 46  ? 23.707 10.064  -0.931  0.30 11.77 ?  46  GLY   A CA   1 
ATOM   1208 C  C    A GLY   A 1 46  ? 22.104 9.802   -0.613  0.70 12.91 ?  46  GLY   A C    1 
ATOM   1209 C  C    B GLY   A 1 46  ? 22.236 9.991   -0.575  0.30 11.71 ?  46  GLY   A C    1 
ATOM   1210 O  O    A GLY   A 1 46  ? 21.435 10.768  -0.226  0.70 14.23 ?  46  GLY   A O    1 
ATOM   1211 O  O    B GLY   A 1 46  ? 21.612 11.016  -0.285  0.30 12.46 ?  46  GLY   A O    1 
ATOM   1212 H  H    A GLY   A 1 46  ? 24.482 8.238   -1.158  0.70 14.47 ?  46  GLY   A H    1 
ATOM   1213 H  H    B GLY   A 1 46  ? 24.556 8.306   -1.198  0.30 13.87 ?  46  GLY   A H    1 
ATOM   1214 H  HA2  A GLY   A 1 46  ? 23.884 10.747  -0.397  0.70 15.26 ?  46  GLY   A HA2  1 
ATOM   1215 H  HA2  B GLY   A 1 46  ? 24.088 10.844  -0.490  0.30 14.11 ?  46  GLY   A HA2  1 
ATOM   1216 H  HA3  A GLY   A 1 46  ? 23.689 10.159  -1.836  0.70 15.26 ?  46  GLY   A HA3  1 
ATOM   1217 H  HA3  B GLY   A 1 46  ? 23.764 10.205  -1.886  0.30 14.11 ?  46  GLY   A HA3  1 
ATOM   1218 N  N    A GLY   A 1 47  ? 21.571 8.601   -0.823  0.70 12.68 ?  47  GLY   A N    1 
ATOM   1219 N  N    B GLY   A 1 47  ? 21.663 8.796   -0.625  0.30 11.46 ?  47  GLY   A N    1 
ATOM   1220 C  CA   A GLY   A 1 47  ? 20.139 8.393   -0.768  0.70 12.41 ?  47  GLY   A CA   1 
ATOM   1221 C  CA   B GLY   A 1 47  ? 20.253 8.620   -0.362  0.30 11.54 ?  47  GLY   A CA   1 
ATOM   1222 C  C    A GLY   A 1 47  ? 19.814 6.967   -0.385  0.70 11.87 ?  47  GLY   A C    1 
ATOM   1223 C  C    B GLY   A 1 47  ? 19.936 7.172   -0.057  0.30 11.25 ?  47  GLY   A C    1 
ATOM   1224 O  O    A GLY   A 1 47  ? 20.703 6.139   -0.175  0.70 12.02 ?  47  GLY   A O    1 
ATOM   1225 O  O    B GLY   A 1 47  ? 20.829 6.334   0.089   0.30 11.34 ?  47  GLY   A O    1 
ATOM   1226 H  H    A GLY   A 1 47  ? 22.023 7.885   -0.984  0.70 15.20 ?  47  GLY   A H    1 
ATOM   1227 H  H    B GLY   A 1 47  ? 22.077 8.076   -0.817  0.30 13.73 ?  47  GLY   A H    1 
ATOM   1228 H  HA2  A GLY   A 1 47  ? 19.741 8.992   -0.118  0.70 14.88 ?  47  GLY   A HA2  1 
ATOM   1229 H  HA2  B GLY   A 1 47  ? 19.983 9.167   0.396   0.30 13.83 ?  47  GLY   A HA2  1 
ATOM   1230 H  HA3  A GLY   A 1 47  ? 19.748 8.567   -1.636  0.70 14.88 ?  47  GLY   A HA3  1 
ATOM   1231 H  HA3  B GLY   A 1 47  ? 19.741 8.905   -1.139  0.30 13.83 ?  47  GLY   A HA3  1 
ATOM   1232 N  N    A GLY   A 1 48  ? 18.518 6.675   -0.313  0.70 12.12 ?  48  GLY   A N    1 
ATOM   1233 N  N    B GLY   A 1 48  ? 18.641 6.888   0.046   0.30 11.64 ?  48  GLY   A N    1 
ATOM   1234 C  CA   A GLY   A 1 48  ? 18.119 5.356   0.118   0.70 12.68 ?  48  GLY   A CA   1 
ATOM   1235 C  CA   B GLY   A 1 48  ? 18.201 5.537   0.338   0.30 11.75 ?  48  GLY   A CA   1 
ATOM   1236 C  C    A GLY   A 1 48  ? 18.615 5.078   1.522   0.70 11.87 ?  48  GLY   A C    1 
ATOM   1237 C  C    B GLY   A 1 48  ? 18.677 5.075   1.698   0.30 11.44 ?  48  GLY   A C    1 
ATOM   1238 O  O    A GLY   A 1 48  ? 18.815 5.992   2.336   0.70 12.02 ?  48  GLY   A O    1 
ATOM   1239 O  O    B GLY   A 1 48  ? 18.757 5.851   2.659   0.30 11.75 ?  48  GLY   A O    1 
ATOM   1240 H  H    A GLY   A 1 48  ? 17.866 7.210   -0.492  0.70 14.53 ?  48  GLY   A H    1 
ATOM   1241 H  H    B GLY   A 1 48  ? 18.009 7.455   -0.045  0.30 13.95 ?  48  GLY   A H    1 
ATOM   1242 H  HA2  A GLY   A 1 48  ? 17.154 5.274   0.107   0.70 15.20 ?  48  GLY   A HA2  1 
ATOM   1243 H  HA2  B GLY   A 1 48  ? 17.233 5.502   0.315   0.30 14.08 ?  48  GLY   A HA2  1 
ATOM   1244 H  HA3  A GLY   A 1 48  ? 18.498 4.689   -0.475  0.70 15.20 ?  48  GLY   A HA3  1 
ATOM   1245 H  HA3  B GLY   A 1 48  ? 18.550 4.926   -0.330  0.30 14.08 ?  48  GLY   A HA3  1 
ATOM   1246 N  N    A VAL   A 1 49  ? 18.820 3.790   1.811   0.70 11.27 ?  49  VAL   A N    1 
ATOM   1247 N  N    B VAL   A 1 49  ? 18.993 3.782   1.784   0.30 10.94 ?  49  VAL   A N    1 
ATOM   1248 C  CA   A VAL   A 1 49  ? 19.335 3.381   3.116   0.70 11.37 ?  49  VAL   A CA   1 
ATOM   1249 C  CA   B VAL   A 1 49  ? 19.544 3.226   3.016   0.30 10.37 ?  49  VAL   A CA   1 
ATOM   1250 C  C    A VAL   A 1 49  ? 20.646 4.088   3.433   0.70 10.48 ?  49  VAL   A C    1 
ATOM   1251 C  C    B VAL   A 1 49  ? 20.810 3.973   3.413   0.30 9.64  ?  49  VAL   A C    1 
ATOM   1252 O  O    A VAL   A 1 49  ? 20.856 4.541   4.562   0.70 10.99 ?  49  VAL   A O    1 
ATOM   1253 O  O    B VAL   A 1 49  ? 20.992 4.342   4.578   0.30 9.66  ?  49  VAL   A O    1 
ATOM   1254 C  CB   A VAL   A 1 49  ? 19.486 1.846   3.171   0.70 12.37 ?  49  VAL   A CB   1 
ATOM   1255 C  CB   B VAL   A 1 49  ? 19.811 1.719   2.853   0.30 9.84  ?  49  VAL   A CB   1 
ATOM   1256 C  CG1  A VAL   A 1 49  ? 20.301 1.416   4.388   0.70 12.50 ?  49  VAL   A CG1  1 
ATOM   1257 C  CG1  B VAL   A 1 49  ? 20.655 1.205   4.012   0.30 9.63  ?  49  VAL   A CG1  1 
ATOM   1258 C  CG2  A VAL   A 1 49  ? 18.115 1.182   3.186   0.70 14.08 ?  49  VAL   A CG2  1 
ATOM   1259 C  CG2  B VAL   A 1 49  ? 18.505 0.942   2.748   0.30 9.91  ?  49  VAL   A CG2  1 
ATOM   1260 H  H    A VAL   A 1 49  ? 18.676 3.133   1.271   0.70 13.51 ?  49  VAL   A H    1 
ATOM   1261 H  H    B VAL   A 1 49  ? 18.910 3.216   1.146   0.30 13.11 ?  49  VAL   A H    1 
ATOM   1262 H  HA   A VAL   A 1 49  ? 18.699 3.632   3.797   0.70 13.63 ?  49  VAL   A HA   1 
ATOM   1263 H  HA   B VAL   A 1 49  ? 18.900 3.337   3.731   0.30 12.42 ?  49  VAL   A HA   1 
ATOM   1264 H  HB   A VAL   A 1 49  ? 19.960 1.544   2.379   0.70 14.83 ?  49  VAL   A HB   1 
ATOM   1265 H  HB   B VAL   A 1 49  ? 20.310 1.576   2.034   0.30 11.79 ?  49  VAL   A HB   1 
ATOM   1266 H  HG11 A VAL   A 1 49  ? 20.151 0.473   4.548   0.70 14.98 ?  49  VAL   A HG11 1 
ATOM   1267 H  HG11 B VAL   A 1 49  ? 20.560 0.244   4.070   0.30 11.54 ?  49  VAL   A HG11 1 
ATOM   1268 H  HG12 A VAL   A 1 49  ? 21.242 1.577   4.216   0.70 14.98 ?  49  VAL   A HG12 1 
ATOM   1269 H  HG12 B VAL   A 1 49  ? 21.586 1.433   3.854   0.30 11.54 ?  49  VAL   A HG12 1 
ATOM   1270 H  HG13 A VAL   A 1 49  ? 20.011 1.932   5.157   0.70 14.98 ?  49  VAL   A HG13 1 
ATOM   1271 H  HG13 B VAL   A 1 49  ? 20.346 1.616   4.833   0.30 11.54 ?  49  VAL   A HG13 1 
ATOM   1272 H  HG21 A VAL   A 1 49  ? 18.229 0.221   3.216   0.70 16.88 ?  49  VAL   A HG21 1 
ATOM   1273 H  HG21 B VAL   A 1 49  ? 18.706 0.003   2.608   0.30 11.88 ?  49  VAL   A HG21 1 
ATOM   1274 H  HG22 A VAL   A 1 49  ? 17.630 1.484   3.971   0.70 16.88 ?  49  VAL   A HG22 1 
ATOM   1275 H  HG22 B VAL   A 1 49  ? 18.006 1.052   3.573   0.30 11.88 ?  49  VAL   A HG22 1 
ATOM   1276 H  HG23 A VAL   A 1 49  ? 17.636 1.436   2.383   0.70 16.88 ?  49  VAL   A HG23 1 
ATOM   1277 H  HG23 B VAL   A 1 49  ? 17.992 1.286   2.001   0.30 11.88 ?  49  VAL   A HG23 1 
ATOM   1278 N  N    A ALA   A 1 50  ? 21.558 4.154   2.458   0.70 10.09 ?  50  ALA   A N    1 
ATOM   1279 N  N    B ALA   A 1 50  ? 21.714 4.182   2.453   0.30 9.33  ?  50  ALA   A N    1 
ATOM   1280 C  CA   A ALA   A 1 50  ? 22.886 4.709   2.712   0.70 9.99  ?  50  ALA   A CA   1 
ATOM   1281 C  CA   B ALA   A 1 50  ? 23.011 4.772   2.769   0.30 9.25  ?  50  ALA   A CA   1 
ATOM   1282 C  C    A ALA   A 1 50  ? 22.799 6.166   3.135   0.70 10.01 ?  50  ALA   A C    1 
ATOM   1283 C  C    B ALA   A 1 50  ? 22.865 6.227   3.190   0.30 9.50  ?  50  ALA   A C    1 
ATOM   1284 O  O    A ALA   A 1 50  ? 23.446 6.581   4.102   0.70 10.42 ?  50  ALA   A O    1 
ATOM   1285 O  O    B ALA   A 1 50  ? 23.467 6.661   4.178   0.30 9.79  ?  50  ALA   A O    1 
ATOM   1286 C  CB   A ALA   A 1 50  ? 23.752 4.578   1.461   0.70 10.05 ?  50  ALA   A CB   1 
ATOM   1287 C  CB   B ALA   A 1 50  ? 23.949 4.649   1.568   0.30 9.06  ?  50  ALA   A CB   1 
ATOM   1288 H  H    A ALA   A 1 50  ? 21.436 3.886   1.650   0.70 12.10 ?  50  ALA   A H    1 
ATOM   1289 H  H    B ALA   A 1 50  ? 21.598 3.993   1.621   0.30 11.18 ?  50  ALA   A H    1 
ATOM   1290 H  HA   A ALA   A 1 50  ? 23.311 4.216   3.431   0.70 11.98 ?  50  ALA   A HA   1 
ATOM   1291 H  HA   B ALA   A 1 50  ? 23.405 4.291   3.509   0.30 11.08 ?  50  ALA   A HA   1 
ATOM   1292 H  HB1  A ALA   A 1 50  ? 24.629 4.952   1.643   0.70 12.04 ?  50  ALA   A HB1  1 
ATOM   1293 H  HB1  B ALA   A 1 50  ? 24.807 5.038   1.798   0.30 10.86 ?  50  ALA   A HB1  1 
ATOM   1294 H  HB2  A ALA   A 1 50  ? 23.832 3.642   1.229   0.70 12.04 ?  50  ALA   A HB2  1 
ATOM   1295 H  HB2  B ALA   A 1 50  ? 24.059 3.710   1.350   0.30 10.86 ?  50  ALA   A HB2  1 
ATOM   1296 H  HB3  A ALA   A 1 50  ? 23.330 5.066   0.735   0.70 12.04 ?  50  ALA   A HB3  1 
ATOM   1297 H  HB3  B ALA   A 1 50  ? 23.562 5.121   0.814   0.30 10.86 ?  50  ALA   A HB3  1 
ATOM   1298 N  N    A GLY   A 1 51  ? 22.013 6.964   2.412   0.70 10.42 ?  51  GLY   A N    1 
ATOM   1299 N  N    B GLY   A 1 51  ? 22.069 6.999   2.449   0.30 10.00 ?  51  GLY   A N    1 
ATOM   1300 C  CA   A GLY   A 1 51  ? 21.865 8.357   2.793   0.70 10.67 ?  51  GLY   A CA   1 
ATOM   1301 C  CA   B GLY   A 1 51  ? 21.872 8.391   2.813   0.30 10.29 ?  51  GLY   A CA   1 
ATOM   1302 C  C    A GLY   A 1 51  ? 21.268 8.504   4.177   0.70 10.46 ?  51  GLY   A C    1 
ATOM   1303 C  C    B GLY   A 1 51  ? 21.230 8.542   4.176   0.30 10.49 ?  51  GLY   A C    1 
ATOM   1304 O  O    A GLY   A 1 51  ? 21.674 9.378   4.949   0.70 11.27 ?  51  GLY   A O    1 
ATOM   1305 O  O    B GLY   A 1 51  ? 21.570 9.454   4.935   0.30 10.85 ?  51  GLY   A O    1 
ATOM   1306 H  H    A GLY   A 1 51  ? 21.577 6.729   1.708   0.70 12.49 ?  51  GLY   A H    1 
ATOM   1307 H  H    B GLY   A 1 51  ? 21.643 6.746   1.746   0.30 11.99 ?  51  GLY   A H    1 
ATOM   1308 H  HA2  A GLY   A 1 51  ? 22.730 8.794   2.779   0.70 12.78 ?  51  GLY   A HA2  1 
ATOM   1309 H  HA2  B GLY   A 1 51  ? 22.727 8.847   2.823   0.30 12.33 ?  51  GLY   A HA2  1 
ATOM   1310 H  HA3  A GLY   A 1 51  ? 21.283 8.806   2.156   0.70 12.78 ?  51  GLY   A HA3  1 
ATOM   1311 H  HA3  B GLY   A 1 51  ? 21.302 8.823   2.157   0.30 12.33 ?  51  GLY   A HA3  1 
ATOM   1312 N  N    . ALA   A 1 52  ? 20.292 7.649   4.508   1.00 10.73 ?  52  ALA   A N    1 
ATOM   1313 C  CA   . ALA   A 1 52  ? 19.644 7.714   5.815   1.00 11.30 ?  52  ALA   A CA   1 
ATOM   1314 C  C    . ALA   A 1 52  ? 20.597 7.301   6.935   1.00 10.65 ?  52  ALA   A C    1 
ATOM   1315 O  O    . ALA   A 1 52  ? 20.669 7.959   7.978   1.00 11.73 ?  52  ALA   A O    1 
ATOM   1316 C  CB   . ALA   A 1 52  ? 18.384 6.846   5.810   1.00 13.16 ?  52  ALA   A CB   1 
ATOM   1317 H  H    A ALA   A 1 52  ? 20.000 7.019   3.994   0.70 12.86 ?  52  ALA   A H    1 
ATOM   1318 H  H    B ALA   A 1 52  ? 20.028 7.000   4.002   0.30 12.86 ?  52  ALA   A H    1 
ATOM   1319 H  HA   . ALA   A 1 52  ? 19.371 8.624   5.977   1.00 13.55 ?  52  ALA   A HA   1 
ATOM   1320 H  HB1  . ALA   A 1 52  ? 17.939 6.934   6.668   1.00 15.78 ?  52  ALA   A HB1  1 
ATOM   1321 H  HB2  . ALA   A 1 52  ? 17.794 7.153   5.102   1.00 15.78 ?  52  ALA   A HB2  1 
ATOM   1322 H  HB3  . ALA   A 1 52  ? 18.631 5.922   5.656   1.00 15.78 ?  52  ALA   A HB3  1 
ATOM   1323 N  N    . LEU   A 1 53  ? 21.329 6.199   6.754   1.00 10.56 ?  53  LEU   A N    1 
ATOM   1324 C  CA   . LEU   A 1 53  ? 22.297 5.795   7.772   1.00 10.79 ?  53  LEU   A CA   1 
ATOM   1325 C  C    . LEU   A 1 53  ? 23.344 6.878   7.974   1.00 10.35 ?  53  LEU   A C    1 
ATOM   1326 O  O    . LEU   A 1 53  ? 23.671 7.239   9.108   1.00 11.56 ?  53  LEU   A O    1 
ATOM   1327 C  CB   . LEU   A 1 53  ? 22.974 4.469   7.394   1.00 11.19 ?  53  LEU   A CB   1 
ATOM   1328 C  CG   . LEU   A 1 53  ? 22.129 3.188   7.477   1.00 11.85 ?  53  LEU   A CG   1 
ATOM   1329 C  CD1  . LEU   A 1 53  ? 22.888 2.023   6.861   1.00 12.76 ?  53  LEU   A CD1  1 
ATOM   1330 C  CD2  . LEU   A 1 53  ? 21.740 2.863   8.910   1.00 13.22 ?  53  LEU   A CD2  1 
ATOM   1331 H  H    . LEU   A 1 53  ? 21.284 5.677   6.069   1.00 12.66 ?  53  LEU   A H    1 
ATOM   1332 H  HA   . LEU   A 1 53  ? 21.835 5.665   8.613   1.00 12.93 ?  53  LEU   A HA   1 
ATOM   1333 H  HB2  . LEU   A 1 53  ? 23.287 4.541   6.477   1.00 13.42 ?  53  LEU   A HB2  1 
ATOM   1334 H  HB3  . LEU   A 1 53  ? 23.735 4.339   7.979   1.00 13.42 ?  53  LEU   A HB3  1 
ATOM   1335 H  HG   . LEU   A 1 53  ? 21.315 3.311   6.961   1.00 14.20 ?  53  LEU   A HG   1 
ATOM   1336 H  HD11 . LEU   A 1 53  ? 22.339 1.224   6.922   1.00 15.29 ?  53  LEU   A HD11 1 
ATOM   1337 H  HD12 . LEU   A 1 53  ? 23.076 2.224   5.931   1.00 15.29 ?  53  LEU   A HD12 1 
ATOM   1338 H  HD13 . LEU   A 1 53  ? 23.715 1.895   7.348   1.00 15.29 ?  53  LEU   A HD13 1 
ATOM   1339 H  HD21 . LEU   A 1 53  ? 21.093 2.141   8.907   1.00 15.85 ?  53  LEU   A HD21 1 
ATOM   1340 H  HD22 . LEU   A 1 53  ? 22.534 2.594   9.398   1.00 15.85 ?  53  LEU   A HD22 1 
ATOM   1341 H  HD23 . LEU   A 1 53  ? 21.353 3.651   9.321   1.00 15.85 ?  53  LEU   A HD23 1 
ATOM   1342 N  N    A ASN   A 1 54  ? 23.887 7.400   6.880   0.70 10.16 ?  54  ASN   A N    1 
ATOM   1343 N  N    B ASN   A 1 54  ? 23.877 7.425   6.881   0.30 10.20 ?  54  ASN   A N    1 
ATOM   1344 C  CA   A ASN   A 1 54  ? 24.936 8.396   7.011   0.70 10.21 ?  54  ASN   A CA   1 
ATOM   1345 C  CA   B ASN   A 1 54  ? 24.916 8.439   7.018   0.30 10.21 ?  54  ASN   A CA   1 
ATOM   1346 C  C    A ASN   A 1 54  ? 24.422 9.655   7.706   0.70 10.40 ?  54  ASN   A C    1 
ATOM   1347 C  C    B ASN   A 1 54  ? 24.398 9.657   7.776   0.30 10.46 ?  54  ASN   A C    1 
ATOM   1348 O  O    A ASN   A 1 54  ? 25.120 10.240  8.543   0.70 11.10 ?  54  ASN   A O    1 
ATOM   1349 O  O    B ASN   A 1 54  ? 25.056 10.154  8.698   0.30 10.62 ?  54  ASN   A O    1 
ATOM   1350 C  CB   A ASN   A 1 54  ? 25.509 8.733   5.648   0.70 10.41 ?  54  ASN   A CB   1 
ATOM   1351 C  CB   B ASN   A 1 54  ? 25.470 8.845   5.655   0.30 9.89  ?  54  ASN   A CB   1 
ATOM   1352 C  CG   A ASN   A 1 54  ? 26.540 9.820   5.744   0.70 10.73 ?  54  ASN   A CG   1 
ATOM   1353 C  CG   B ASN   A 1 54  ? 26.464 9.987   5.764   0.30 9.75  ?  54  ASN   A CG   1 
ATOM   1354 O  OD1  A ASN   A 1 54  ? 27.515 9.691   6.496   0.70 10.41 ?  54  ASN   A OD1  1 
ATOM   1355 O  OD1  B ASN   A 1 54  ? 27.544 9.829   6.338   0.30 10.46 ?  54  ASN   A OD1  1 
ATOM   1356 N  ND2  A ASN   A 1 54  ? 26.331 10.911  5.021   0.70 11.29 ?  54  ASN   A ND2  1 
ATOM   1357 N  ND2  B ASN   A 1 54  ? 26.099 11.150  5.237   0.30 9.52  ?  54  ASN   A ND2  1 
ATOM   1358 H  H    A ASN   A 1 54  ? 23.661 7.201   6.073   0.70 12.18 ?  54  ASN   A H    1 
ATOM   1359 H  H    B ASN   A 1 54  ? 23.652 7.236   6.072   0.30 12.23 ?  54  ASN   A H    1 
ATOM   1360 H  HA   A ASN   A 1 54  ? 25.644 8.024   7.555   0.70 12.24 ?  54  ASN   A HA   1 
ATOM   1361 H  HA   B ASN   A 1 54  ? 25.643 8.066   7.533   0.30 12.23 ?  54  ASN   A HA   1 
ATOM   1362 H  HB2  A ASN   A 1 54  ? 25.933 7.935   5.280   0.70 12.48 ?  54  ASN   A HB2  1 
ATOM   1363 H  HB2  B ASN   A 1 54  ? 25.928 8.082   5.260   0.30 11.86 ?  54  ASN   A HB2  1 
ATOM   1364 H  HB3  A ASN   A 1 54  ? 24.799 9.032   5.065   0.70 12.48 ?  54  ASN   A HB3  1 
ATOM   1365 H  HB3  B ASN   A 1 54  ? 24.743 9.129   5.082   0.30 11.86 ?  54  ASN   A HB3  1 
ATOM   1366 H  HD21 A ASN   A 1 54  ? 26.899 11.552  5.048   0.70 13.53 ?  54  ASN   A HD21 1 
ATOM   1367 H  HD21 B ASN   A 1 54  ? 26.630 11.826  5.279   0.30 11.41 ?  54  ASN   A HD21 1 
ATOM   1368 H  HD22 A ASN   A 1 54  ? 25.639 10.962  4.516   0.70 13.53 ?  54  ASN   A HD22 1 
ATOM   1369 H  HD22 B ASN   A 1 54  ? 25.337 11.225  4.848   0.30 11.41 ?  54  ASN   A HD22 1 
ATOM   1370 N  N    A LYS   A 1 55  ? 23.201 10.088  7.375   0.70 10.91 ?  55  LYS   A N    1 
ATOM   1371 N  N    B LYS   A 1 55  ? 23.210 10.147  7.409   0.30 10.80 ?  55  LYS   A N    1 
ATOM   1372 C  CA   A LYS   A 1 55  ? 22.610 11.245  8.038   0.70 11.53 ?  55  LYS   A CA   1 
ATOM   1373 C  CA   B LYS   A 1 55  ? 22.651 11.311  8.090   0.30 11.49 ?  55  LYS   A CA   1 
ATOM   1374 C  C    A LYS   A 1 55  ? 22.537 11.031  9.544   0.70 11.70 ?  55  LYS   A C    1 
ATOM   1375 C  C    B LYS   A 1 55  ? 22.510 11.053  9.584   0.30 11.76 ?  55  LYS   A C    1 
ATOM   1376 O  O    A LYS   A 1 55  ? 22.842 11.939  10.329  0.70 12.59 ?  55  LYS   A O    1 
ATOM   1377 O  O    B LYS   A 1 55  ? 22.736 11.955  10.402  0.30 12.00 ?  55  LYS   A O    1 
ATOM   1378 C  CB   A LYS   A 1 55  ? 21.225 11.506  7.442   0.70 12.31 ?  55  LYS   A CB   1 
ATOM   1379 C  CB   B LYS   A 1 55  ? 21.307 11.688  7.464   0.30 12.31 ?  55  LYS   A CB   1 
ATOM   1380 C  CG   A LYS   A 1 55  ? 20.467 12.681  8.043   0.70 13.61 ?  55  LYS   A CG   1 
ATOM   1381 C  CG   B LYS   A 1 55  ? 20.566 12.813  8.183   0.30 13.44 ?  55  LYS   A CG   1 
ATOM   1382 C  CD   A LYS   A 1 55  ? 19.126 12.863  7.334   0.70 14.77 ?  55  LYS   A CD   1 
ATOM   1383 C  CD   B LYS   A 1 55  ? 19.257 13.150  7.482   0.30 14.65 ?  55  LYS   A CD   1 
ATOM   1384 C  CE   A LYS   A 1 55  ? 18.298 13.982  7.946   0.70 16.63 ?  55  LYS   A CE   1 
ATOM   1385 C  CE   B LYS   A 1 55  ? 18.391 14.080  8.322   0.30 16.17 ?  55  LYS   A CE   1 
ATOM   1386 N  NZ   A LYS   A 1 55  ? 16.962 14.090  7.297   0.70 17.28 ?  55  LYS   A NZ   1 
ATOM   1387 N  NZ   B LYS   A 1 55  ? 17.068 14.338  7.687   0.30 16.82 ?  55  LYS   A NZ   1 
ATOM   1388 H  H    A LYS   A 1 55  ? 22.696 9.722   6.778   0.70 13.08 ?  55  LYS   A H    1 
ATOM   1389 H  H    B LYS   A 1 55  ? 22.710 9.824   6.785   0.30 12.94 ?  55  LYS   A H    1 
ATOM   1390 H  HA   A LYS   A 1 55  ? 23.162 12.020  7.870   0.70 13.82 ?  55  LYS   A HA   1 
ATOM   1391 H  HA   B LYS   A 1 55  ? 23.251 12.062  7.974   0.30 13.78 ?  55  LYS   A HA   1 
ATOM   1392 H  HB2  A LYS   A 1 55  ? 21.324 11.682  6.494   0.70 14.76 ?  55  LYS   A HB2  1 
ATOM   1393 H  HB2  B LYS   A 1 55  ? 21.460 11.979  6.550   0.30 14.75 ?  55  LYS   A HB2  1 
ATOM   1394 H  HB3  A LYS   A 1 55  ? 20.677 10.714  7.569   0.70 14.76 ?  55  LYS   A HB3  1 
ATOM   1395 H  HB3  B LYS   A 1 55  ? 20.730 10.910  7.466   0.30 14.75 ?  55  LYS   A HB3  1 
ATOM   1396 H  HG2  A LYS   A 1 55  ? 20.294 12.511  8.983   0.70 16.32 ?  55  LYS   A HG2  1 
ATOM   1397 H  HG2  B LYS   A 1 55  ? 20.356 12.536  9.089   0.30 16.12 ?  55  LYS   A HG2  1 
ATOM   1398 H  HG3  A LYS   A 1 55  ? 20.984 13.492  7.933   0.70 16.32 ?  55  LYS   A HG3  1 
ATOM   1399 H  HG3  B LYS   A 1 55  ? 21.120 13.609  8.193   0.30 16.12 ?  55  LYS   A HG3  1 
ATOM   1400 H  HD2  A LYS   A 1 55  ? 19.286 13.078  6.402   0.70 17.71 ?  55  LYS   A HD2  1 
ATOM   1401 H  HD2  B LYS   A 1 55  ? 19.450 13.594  6.641   0.30 17.56 ?  55  LYS   A HD2  1 
ATOM   1402 H  HD3  A LYS   A 1 55  ? 18.617 12.038  7.402   0.70 17.71 ?  55  LYS   A HD3  1 
ATOM   1403 H  HD3  B LYS   A 1 55  ? 18.760 12.333  7.322   0.30 17.56 ?  55  LYS   A HD3  1 
ATOM   1404 H  HE2  A LYS   A 1 55  ? 18.166 13.801  8.890   0.70 19.94 ?  55  LYS   A HE2  1 
ATOM   1405 H  HE2  B LYS   A 1 55  ? 18.236 13.671  9.189   0.30 19.39 ?  55  LYS   A HE2  1 
ATOM   1406 H  HE3  A LYS   A 1 55  ? 18.766 14.824  7.828   0.70 19.94 ?  55  LYS   A HE3  1 
ATOM   1407 H  HE3  B LYS   A 1 55  ? 18.846 14.929  8.430   0.30 19.39 ?  55  LYS   A HE3  1 
ATOM   1408 H  HZ1  A LYS   A 1 55  ? 16.391 14.497  7.846   0.70 20.71 ?  55  LYS   A HZ1  1 
ATOM   1409 H  HZ1  B LYS   A 1 55  ? 16.584 14.882  8.200   0.30 20.17 ?  55  LYS   A HZ1  1 
ATOM   1410 H  HZ2  A LYS   A 1 55  ? 17.026 14.565  6.546   0.70 20.71 ?  55  LYS   A HZ2  1 
ATOM   1411 H  HZ2  B LYS   A 1 55  ? 17.180 14.718  6.890   0.30 20.17 ?  55  LYS   A HZ2  1 
ATOM   1412 H  HZ3  A LYS   A 1 55  ? 16.649 13.280  7.103   0.70 20.71 ?  55  LYS   A HZ3  1 
ATOM   1413 H  HZ3  B LYS   A 1 55  ? 16.624 13.572  7.582   0.30 20.17 ?  55  LYS   A HZ3  1 
ATOM   1414 N  N    . ALA   A 1 56  ? 22.146 9.825   9.965   1.00 12.03 ?  56  ALA   A N    1 
ATOM   1415 C  CA   . ALA   A 1 56  ? 22.016 9.510   11.381  1.00 12.65 ?  56  ALA   A CA   1 
ATOM   1416 C  C    . ALA   A 1 56  ? 23.355 9.538   12.108  1.00 12.45 ?  56  ALA   A C    1 
ATOM   1417 O  O    . ALA   A 1 56  ? 23.375 9.730   13.325  1.00 14.01 ?  56  ALA   A O    1 
ATOM   1418 C  CB   . ALA   A 1 56  ? 21.312 8.162   11.567  1.00 13.62 ?  56  ALA   A CB   1 
ATOM   1419 H  H    A ALA   A 1 56  ? 21.950 9.172   9.442   0.70 14.42 ?  56  ALA   A H    1 
ATOM   1420 H  H    B ALA   A 1 56  ? 21.971 9.175   9.432   0.30 14.42 ?  56  ALA   A H    1 
ATOM   1421 H  HA   . ALA   A 1 56  ? 21.460 10.180  11.795  1.00 15.17 ?  56  ALA   A HA   1 
ATOM   1422 H  HB1  . ALA   A 1 56  ? 21.239 7.971   12.518  1.00 16.33 ?  56  ALA   A HB1  1 
ATOM   1423 H  HB2  . ALA   A 1 56  ? 20.427 8.212   11.173  1.00 16.33 ?  56  ALA   A HB2  1 
ATOM   1424 H  HB3  . ALA   A 1 56  ? 21.829 7.467   11.132  1.00 16.33 ?  56  ALA   A HB3  1 
ATOM   1425 N  N    . THR   A 1 57  ? 24.468 9.343   11.395  1.00 11.79 ?  57  THR   A N    1 
ATOM   1426 C  CA   . THR   A 1 57  ? 25.809 9.471   11.972  1.00 11.79 ?  57  THR   A CA   1 
ATOM   1427 C  C    . THR   A 1 57  ? 26.363 10.890  11.888  1.00 12.25 ?  57  THR   A C    1 
ATOM   1428 O  O    . THR   A 1 57  ? 27.552 11.100  12.172  1.00 12.75 ?  57  THR   A O    1 
ATOM   1429 C  CB   . THR   A 1 57  ? 26.822 8.522   11.303  1.00 11.79 ?  57  THR   A CB   1 
ATOM   1430 O  OG1  . THR   A 1 57  ? 27.203 9.023   10.009  1.00 11.47 ?  57  THR   A OG1  1 
ATOM   1431 C  CG2  . THR   A 1 57  ? 26.285 7.105   11.185  1.00 11.77 ?  57  THR   A CG2  1 
ATOM   1432 H  H    . THR   A 1 57  ? 24.474 9.112   10.566  1.00 14.13 ?  57  THR   A H    1 
ATOM   1433 H  HA   . THR   A 1 57  ? 25.765 9.216   12.913  1.00 14.14 ?  57  THR   A HA   1 
ATOM   1434 H  HB   . THR   A 1 57  ? 27.617 8.475   11.860  1.00 14.13 ?  57  THR   A HB   1 
ATOM   1435 H  HG1  . THR   A 1 57  ? 26.526 9.094   9.520   1.00 13.75 ?  57  THR   A HG1  1 
ATOM   1436 H  HG21 . THR   A 1 57  ? 26.971 6.509   10.840  1.00 14.11 ?  57  THR   A HG21 1 
ATOM   1437 H  HG22 . THR   A 1 57  ? 25.998 6.779   12.053  1.00 14.11 ?  57  THR   A HG22 1 
ATOM   1438 H  HG23 . THR   A 1 57  ? 25.525 7.083   10.579  1.00 14.11 ?  57  THR   A HG23 1 
ATOM   1439 N  N    . ASN   A 1 58  ? 25.547 11.863  11.483  1.00 12.77 ?  58  ASN   A N    1 
ATOM   1440 C  CA   . ASN   A 1 58  ? 26.014 13.243  11.382  1.00 13.58 ?  58  ASN   A CA   1 
ATOM   1441 C  C    . ASN   A 1 58  ? 27.166 13.367  10.378  1.00 12.28 ?  58  ASN   A C    1 
ATOM   1442 O  O    . ASN   A 1 58  ? 28.061 14.202  10.536  1.00 13.06 ?  58  ASN   A O    1 
ATOM   1443 C  CB   . ASN   A 1 58  ? 26.379 13.781  12.779  1.00 16.46 ?  58  ASN   A CB   1 
ATOM   1444 C  CG   . ASN   A 1 58  ? 26.806 15.231  12.773  1.00 20.32 ?  58  ASN   A CG   1 
ATOM   1445 O  OD1  . ASN   A 1 58  ? 26.183 16.066  12.128  1.00 22.03 ?  58  ASN   A OD1  1 
ATOM   1446 N  ND2  . ASN   A 1 58  ? 27.869 15.543  13.514  1.00 21.60 ?  58  ASN   A ND2  1 
ATOM   1447 H  H    . ASN   A 1 58  ? 24.723 11.740  11.254  1.00 15.31 ?  58  ASN   A H    1 
ATOM   1448 H  HA   . ASN   A 1 58  ? 25.282 13.776  11.049  1.00 16.28 ?  58  ASN   A HA   1 
ATOM   1449 H  HB2  . ASN   A 1 58  ? 25.600 13.694  13.362  1.00 19.74 ?  58  ASN   A HB2  1 
ATOM   1450 H  HB3  . ASN   A 1 58  ? 27.111 13.262  13.142  1.00 19.74 ?  58  ASN   A HB3  1 
ATOM   1451 H  HD21 . ASN   A 1 58  ? 28.143 16.359  13.548  1.00 25.91 ?  58  ASN   A HD21 1 
ATOM   1452 H  HD22 . ASN   A 1 58  ? 28.275 14.932  13.955  1.00 25.91 ?  58  ASN   A HD22 1 
ATOM   1453 N  N    . ASN   A 1 59  ? 27.148 12.545  9.326   1.00 11.34 ?  59  ASN   A N    1 
ATOM   1454 C  CA   . ASN   A 1 59  ? 28.130 12.516  8.236   1.00 11.40 ?  59  ASN   A CA   1 
ATOM   1455 C  C    . ASN   A 1 59  ? 29.444 11.831  8.626   1.00 10.89 ?  59  ASN   A C    1 
ATOM   1456 O  O    . ASN   A 1 59  ? 30.366 11.783  7.799   1.00 11.28 ?  59  ASN   A O    1 
ATOM   1457 C  CB   . ASN   A 1 59  ? 28.421 13.900  7.627   1.00 11.44 ?  59  ASN   A CB   1 
ATOM   1458 C  CG   . ASN   A 1 59  ? 28.778 13.829  6.159   1.00 11.69 ?  59  ASN   A CG   1 
ATOM   1459 O  OD1  . ASN   A 1 59  ? 28.071 13.210  5.359   1.00 12.10 ?  59  ASN   A OD1  1 
ATOM   1460 N  ND2  . ASN   A 1 59  ? 29.867 14.497  5.785   1.00 12.28 ?  59  ASN   A ND2  1 
ATOM   1461 H  H    . ASN   A 1 59  ? 26.532 11.954  9.211   1.00 13.59 ?  59  ASN   A H    1 
ATOM   1462 H  HA   . ASN   A 1 59  ? 27.751 11.984  7.523   1.00 13.67 ?  59  ASN   A HA   1 
ATOM   1463 H  HB2  . ASN   A 1 59  ? 27.631 14.460  7.713   1.00 13.71 ?  59  ASN   A HB2  1 
ATOM   1464 H  HB3  . ASN   A 1 59  ? 29.167 14.308  8.093   1.00 13.71 ?  59  ASN   A HB3  1 
ATOM   1465 H  HD21 . ASN   A 1 59  ? 30.117 14.493  4.961   1.00 14.72 ?  59  ASN   A HD21 1 
ATOM   1466 H  HD22 . ASN   A 1 59  ? 30.339 14.923  6.369   1.00 14.72 ?  59  ASN   A HD22 1 
ATOM   1467 N  N    . ALA   A 1 60  ? 29.565 11.288  9.837   1.00 11.20 ?  60  ALA   A N    1 
ATOM   1468 C  CA   . ALA   A 1 60  ? 30.802 10.603  10.193  1.00 11.09 ?  60  ALA   A CA   1 
ATOM   1469 C  C    . ALA   A 1 60  ? 31.027 9.370   9.326   1.00 11.14 ?  60  ALA   A C    1 
ATOM   1470 O  O    . ALA   A 1 60  ? 32.172 9.041   8.996   1.00 11.75 ?  60  ALA   A O    1 
ATOM   1471 C  CB   . ALA   A 1 60  ? 30.791 10.239  11.676  1.00 11.81 ?  60  ALA   A CB   1 
ATOM   1472 H  H    . ALA   A 1 60  ? 28.966 11.300  10.451  1.00 13.42 ?  60  ALA   A H    1 
ATOM   1473 H  HA   . ALA   A 1 60  ? 31.548 11.207  10.044  1.00 13.29 ?  60  ALA   A HA   1 
ATOM   1474 H  HB1  . ALA   A 1 60  ? 31.619 9.788   11.899  1.00 14.15 ?  60  ALA   A HB1  1 
ATOM   1475 H  HB2  . ALA   A 1 60  ? 30.710 11.056  12.200  1.00 14.15 ?  60  ALA   A HB2  1 
ATOM   1476 H  HB3  . ALA   A 1 60  ? 30.036 9.659   11.854  1.00 14.15 ?  60  ALA   A HB3  1 
ATOM   1477 N  N    . MET   A 1 61  ? 29.953 8.677   8.945   1.00 10.91 ?  61  MET   A N    1 
ATOM   1478 C  CA   . MET   A 1 61  ? 30.094 7.540   8.041   1.00 10.53 ?  61  MET   A CA   1 
ATOM   1479 C  C    . MET   A 1 61  ? 30.728 7.965   6.719   1.00 10.63 ?  61  MET   A C    1 
ATOM   1480 O  O    . MET   A 1 61  ? 31.621 7.279   6.204   1.00 11.08 ?  61  MET   A O    1 
ATOM   1481 C  CB   . MET   A 1 61  ? 28.733 6.874   7.829   1.00 10.41 ?  61  MET   A CB   1 
ATOM   1482 C  CG   . MET   A 1 61  ? 28.743 5.713   6.858   1.00 11.17 ?  61  MET   A CG   1 
ATOM   1483 S  SD   . MET   A 1 61  ? 27.117 4.962   6.644   1.00 12.23 ?  61  MET   A SD   1 
ATOM   1484 C  CE   . MET   A 1 61  ? 26.991 4.066   8.199   1.00 13.55 ?  61  MET   A CE   1 
ATOM   1485 H  H    . MET   A 1 61  ? 29.145 8.846   9.186   1.00 13.08 ?  61  MET   A H    1 
ATOM   1486 H  HA   . MET   A 1 61  ? 30.673 6.886   8.460   1.00 12.62 ?  61  MET   A HA   1 
ATOM   1487 H  HB2  . MET   A 1 61  ? 28.415 6.543   8.683   1.00 12.47 ?  61  MET   A HB2  1 
ATOM   1488 H  HB3  . MET   A 1 61  ? 28.113 7.537   7.486   1.00 12.47 ?  61  MET   A HB3  1 
ATOM   1489 H  HG2  . MET   A 1 61  ? 29.027 6.016   5.986   1.00 13.39 ?  61  MET   A HG2  1 
ATOM   1490 H  HG3  . MET   A 1 61  ? 29.339 5.023   7.186   1.00 13.39 ?  61  MET   A HG3  1 
ATOM   1491 H  HE1  . MET   A 1 61  ? 26.149 3.581   8.219   1.00 16.24 ?  61  MET   A HE1  1 
ATOM   1492 H  HE2  . MET   A 1 61  ? 27.731 3.444   8.268   1.00 16.24 ?  61  MET   A HE2  1 
ATOM   1493 H  HE3  . MET   A 1 61  ? 27.021 4.697   8.938   1.00 16.24 ?  61  MET   A HE3  1 
ATOM   1494 N  N    . GLN   A 1 62  ? 30.286 9.095   6.161   1.00 10.79 ?  62  GLN   A N    1 
ATOM   1495 C  CA   . GLN   A 1 62  ? 30.856 9.563   4.901   1.00 10.77 ?  62  GLN   A CA   1 
ATOM   1496 C  C    . GLN   A 1 62  ? 32.327 9.931   5.052   1.00 10.63 ?  62  GLN   A C    1 
ATOM   1497 O  O    . GLN   A 1 62  ? 33.139 9.615   4.176   1.00 10.82 ?  62  GLN   A O    1 
ATOM   1498 C  CB   . GLN   A 1 62  ? 30.056 10.747  4.364   1.00 10.76 ?  62  GLN   A CB   1 
ATOM   1499 C  CG   . GLN   A 1 62  ? 30.435 11.103  2.939   1.00 10.71 ?  62  GLN   A CG   1 
ATOM   1500 C  CD   . GLN   A 1 62  ? 30.106 9.976   1.992   1.00 10.89 ?  62  GLN   A CD   1 
ATOM   1501 O  OE1  . GLN   A 1 62  ? 28.925 9.675   1.776   1.00 11.53 ?  62  GLN   A OE1  1 
ATOM   1502 N  NE2  . GLN   A 1 62  ? 31.126 9.301   1.467   1.00 11.70 ?  62  GLN   A NE2  1 
ATOM   1503 H  H    . GLN   A 1 62  ? 29.666 9.592   6.486   1.00 12.93 ?  62  GLN   A H    1 
ATOM   1504 H  HA   . GLN   A 1 62  ? 30.799 8.841   4.254   1.00 12.91 ?  62  GLN   A HA   1 
ATOM   1505 H  HB2  . GLN   A 1 62  ? 29.112 10.526  4.381   1.00 12.90 ?  62  GLN   A HB2  1 
ATOM   1506 H  HB3  . GLN   A 1 62  ? 30.227 11.522  4.921   1.00 12.90 ?  62  GLN   A HB3  1 
ATOM   1507 H  HG2  . GLN   A 1 62  ? 29.929 11.881  2.661   1.00 12.83 ?  62  GLN   A HG2  1 
ATOM   1508 H  HG3  . GLN   A 1 62  ? 31.383 11.277  2.889   1.00 12.83 ?  62  GLN   A HG3  1 
ATOM   1509 H  HE21 . GLN   A 1 62  ? 31.934 9.529   1.659   1.00 14.03 ?  62  GLN   A HE21 1 
ATOM   1510 H  HE22 . GLN   A 1 62  ? 30.981 8.644   0.932   1.00 14.03 ?  62  GLN   A HE22 1 
ATOM   1511 N  N    . VAL   A 1 63  ? 32.687 10.607  6.145   1.00 11.28 ?  63  VAL   A N    1 
ATOM   1512 C  CA   . VAL   A 1 63  ? 34.079 11.005  6.355   1.00 12.06 ?  63  VAL   A CA   1 
ATOM   1513 C  C    . VAL   A 1 63  ? 34.975 9.771   6.422   1.00 11.42 ?  63  VAL   A C    1 
ATOM   1514 O  O    . VAL   A 1 63  ? 36.028 9.700   5.770   1.00 12.06 ?  63  VAL   A O    1 
ATOM   1515 C  CB   . VAL   A 1 63  ? 34.191 11.880  7.617   1.00 13.54 ?  63  VAL   A CB   1 
ATOM   1516 C  CG1  . VAL   A 1 63  ? 35.646 12.120  7.975   1.00 15.29 ?  63  VAL   A CG1  1 
ATOM   1517 C  CG2  . VAL   A 1 63  ? 33.469 13.214  7.401   1.00 13.69 ?  63  VAL   A CG2  1 
ATOM   1518 H  H    . VAL   A 1 63  ? 32.145 10.847  6.775   1.00 13.52 ?  63  VAL   A H    1 
ATOM   1519 H  HA   . VAL   A 1 63  ? 34.363 11.540  5.599   1.00 14.46 ?  63  VAL   A HA   1 
ATOM   1520 H  HB   . VAL   A 1 63  ? 33.774 11.425  8.363   1.00 16.23 ?  63  VAL   A HB   1 
ATOM   1521 H  HG11 . VAL   A 1 63  ? 35.698 12.855  8.603   1.00 18.33 ?  63  VAL   A HG11 1 
ATOM   1522 H  HG12 . VAL   A 1 63  ? 36.012 11.316  8.375   1.00 18.33 ?  63  VAL   A HG12 1 
ATOM   1523 H  HG13 . VAL   A 1 63  ? 36.136 12.341  7.166   1.00 18.33 ?  63  VAL   A HG13 1 
ATOM   1524 H  HG21 . VAL   A 1 63  ? 33.563 13.758  8.201   1.00 16.41 ?  63  VAL   A HG21 1 
ATOM   1525 H  HG22 . VAL   A 1 63  ? 33.870 13.672  6.644   1.00 16.41 ?  63  VAL   A HG22 1 
ATOM   1526 H  HG23 . VAL   A 1 63  ? 32.533 13.041  7.227   1.00 16.41 ?  63  VAL   A HG23 1 
ATOM   1527 N  N    . GLU   A 1 64  ? 34.550 8.763   7.189   1.00 11.36 ?  64  GLU   A N    1 
ATOM   1528 C  CA   . GLU   A 1 64  ? 35.308 7.523   7.288   1.00 11.50 ?  64  GLU   A CA   1 
ATOM   1529 C  C    . GLU   A 1 64  ? 35.395 6.834   5.934   1.00 11.09 ?  64  GLU   A C    1 
ATOM   1530 O  O    . GLU   A 1 64  ? 36.448 6.293   5.558   1.00 11.68 ?  64  GLU   A O    1 
ATOM   1531 C  CB   . GLU   A 1 64  ? 34.621 6.621   8.312   1.00 12.02 ?  64  GLU   A CB   1 
ATOM   1532 C  CG   . GLU   A 1 64  ? 35.263 5.269   8.460   1.00 12.95 ?  64  GLU   A CG   1 
ATOM   1533 C  CD   . GLU   A 1 64  ? 34.379 4.277   9.188   1.00 13.40 ?  64  GLU   A CD   1 
ATOM   1534 O  OE1  . GLU   A 1 64  ? 33.140 4.370   9.054   1.00 14.19 ?  64  GLU   A OE1  1 
ATOM   1535 O  OE2  . GLU   A 1 64  ? 34.933 3.388   9.876   1.00 13.52 -1 64  GLU   A OE2  1 
ATOM   1536 H  H    . GLU   A 1 64  ? 33.822 8.774   7.649   1.00 13.61 ?  64  GLU   A H    1 
ATOM   1537 H  HA   . GLU   A 1 64  ? 36.207 7.724   7.603   1.00 13.78 ?  64  GLU   A HA   1 
ATOM   1538 H  HB2  . GLU   A 1 64  ? 34.648 7.063   9.182   1.00 14.41 ?  64  GLU   A HB2  1 
ATOM   1539 H  HB3  . GLU   A 1 64  ? 33.699 6.498   8.042   1.00 14.41 ?  64  GLU   A HB3  1 
ATOM   1540 H  HG2  . GLU   A 1 64  ? 35.456 4.904   7.581   1.00 15.52 ?  64  GLU   A HG2  1 
ATOM   1541 H  HG3  . GLU   A 1 64  ? 36.085 5.368   8.962   1.00 15.52 ?  64  GLU   A HG3  1 
ATOM   1542 N  N    . SER   A 1 65  ? 34.282 6.830   5.196   1.00 10.69 ?  65  SER   A N    1 
ATOM   1543 C  CA   . SER   A 1 65  ? 34.234 6.169   3.898   1.00 10.72 ?  65  SER   A CA   1 
ATOM   1544 C  C    . SER   A 1 65  ? 35.161 6.835   2.890   1.00 10.89 ?  65  SER   A C    1 
ATOM   1545 O  O    . SER   A 1 65  ? 35.801 6.153   2.082   1.00 11.96 ?  65  SER   A O    1 
ATOM   1546 C  CB   . SER   A 1 65  ? 32.802 6.180   3.364   1.00 10.74 ?  65  SER   A CB   1 
ATOM   1547 O  OG   . SER   A 1 65  ? 31.941 5.375   4.162   1.00 11.43 ?  65  SER   A OG   1 
ATOM   1548 H  H    . SER   A 1 65  ? 33.548 7.214   5.427   1.00 12.81 ?  65  SER   A H    1 
ATOM   1549 H  HA   . SER   A 1 65  ? 34.514 5.250   3.999   1.00 12.84 ?  65  SER   A HA   1 
ATOM   1550 H  HB2  . SER   A 1 65  ? 32.466 7.087   3.367   1.00 12.87 ?  65  SER   A HB2  1 
ATOM   1551 H  HB3  . SER   A 1 65  ? 32.803 5.829   2.460   1.00 12.87 ?  65  SER   A HB3  1 
ATOM   1552 H  HG   . SER   A 1 65  ? 31.934 5.662   4.956   1.00 13.69 ?  65  SER   A HG   1 
ATOM   1553 N  N    . ASP   A 1 66  ? 35.233 8.168   2.904   1.00 11.14 ?  66  ASP   A N    1 
ATOM   1554 C  CA   . ASP   A 1 66  ? 36.097 8.861   1.955   1.00 12.05 ?  66  ASP   A CA   1 
ATOM   1555 C  C    . ASP   A 1 66  ? 37.559 8.506   2.196   1.00 12.16 ?  66  ASP   A C    1 
ATOM   1556 O  O    . ASP   A 1 66  ? 38.333 8.335   1.246   1.00 12.88 ?  66  ASP   A O    1 
ATOM   1557 C  CB   . ASP   A 1 66  ? 35.876 10.368  2.059   1.00 13.18 ?  66  ASP   A CB   1 
ATOM   1558 C  CG   . ASP   A 1 66  ? 34.545 10.829  1.448   1.00 14.84 ?  66  ASP   A CG   1 
ATOM   1559 O  OD1  . ASP   A 1 66  ? 33.836 10.029  0.799   1.00 15.09 ?  66  ASP   A OD1  1 
ATOM   1560 O  OD2  . ASP   A 1 66  ? 34.241 12.031  1.592   1.00 18.00 -1 66  ASP   A OD2  1 
ATOM   1561 H  H    . ASP   A 1 66  ? 34.794 8.684   3.439   1.00 13.36 ?  66  ASP   A H    1 
ATOM   1562 H  HA   . ASP   A 1 66  ? 35.865 8.587   1.054   1.00 14.44 ?  66  ASP   A HA   1 
ATOM   1563 H  HB2  . ASP   A 1 66  ? 35.874 10.626  2.994   1.00 15.80 ?  66  ASP   A HB2  1 
ATOM   1564 H  HB3  . ASP   A 1 66  ? 36.598 10.826  1.594   1.00 15.80 ?  66  ASP   A HB3  1 
ATOM   1565 N  N    . ASP   A 1 67  ? 37.952 8.376   3.463   1.00 12.33 ?  67  ASP   A N    1 
ATOM   1566 C  CA   . ASP   A 1 67  ? 39.308 7.931   3.765   1.00 12.98 ?  67  ASP   A CA   1 
ATOM   1567 C  C    . ASP   A 1 67  ? 39.533 6.497   3.300   1.00 12.77 ?  67  ASP   A C    1 
ATOM   1568 O  O    . ASP   A 1 67  ? 40.594 6.171   2.753   1.00 13.49 ?  67  ASP   A O    1 
ATOM   1569 C  CB   . ASP   A 1 67  ? 39.576 8.072   5.262   1.00 14.46 ?  67  ASP   A CB   1 
ATOM   1570 C  CG   . ASP   A 1 67  ? 40.872 7.413   5.687   1.00 15.66 ?  67  ASP   A CG   1 
ATOM   1571 O  OD1  . ASP   A 1 67  ? 41.942 8.047   5.553   1.00 18.19 ?  67  ASP   A OD1  1 
ATOM   1572 O  OD2  . ASP   A 1 67  ? 40.821 6.251   6.151   1.00 15.52 -1 67  ASP   A OD2  1 
ATOM   1573 H  H    . ASP   A 1 67  ? 37.465 8.539   4.149   1.00 14.78 ?  67  ASP   A H    1 
ATOM   1574 H  HA   . ASP   A 1 67  ? 39.941 8.497   3.294   1.00 15.57 ?  67  ASP   A HA   1 
ATOM   1575 H  HB2  . ASP   A 1 67  ? 39.630 9.011   5.483   1.00 17.33 ?  67  ASP   A HB2  1 
ATOM   1576 H  HB3  . ASP   A 1 67  ? 38.852 7.651   5.752   1.00 17.33 ?  67  ASP   A HB3  1 
ATOM   1577 N  N    . TYR   A 1 68  ? 38.539 5.621   3.498   1.00 12.61 ?  68  TYR   A N    1 
ATOM   1578 C  CA   . TYR   A 1 68  ? 38.656 4.243   3.022   1.00 12.62 ?  68  TYR   A CA   1 
ATOM   1579 C  C    . TYR   A 1 68  ? 38.900 4.193   1.514   1.00 12.26 ?  68  TYR   A C    1 
ATOM   1580 O  O    . TYR   A 1 68  ? 39.781 3.462   1.040   1.00 12.95 ?  68  TYR   A O    1 
ATOM   1581 C  CB   . TYR   A 1 68  ? 37.405 3.423   3.400   1.00 13.07 ?  68  TYR   A CB   1 
ATOM   1582 C  CG   . TYR   A 1 68  ? 37.430 2.035   2.769   1.00 14.50 ?  68  TYR   A CG   1 
ATOM   1583 C  CD1  . TYR   A 1 68  ? 36.970 1.843   1.468   1.00 15.93 ?  68  TYR   A CD1  1 
ATOM   1584 C  CD2  . TYR   A 1 68  ? 37.962 0.946   3.439   1.00 16.35 ?  68  TYR   A CD2  1 
ATOM   1585 C  CE1  . TYR   A 1 68  ? 37.035 0.626   0.854   1.00 17.14 ?  68  TYR   A CE1  1 
ATOM   1586 C  CE2  . TYR   A 1 68  ? 38.019 -0.315  2.825   1.00 16.78 ?  68  TYR   A CE2  1 
ATOM   1587 C  CZ   . TYR   A 1 68  ? 37.563 -0.448  1.531   1.00 17.32 ?  68  TYR   A CZ   1 
ATOM   1588 O  OH   . TYR   A 1 68  ? 37.638 -1.663  0.903   1.00 18.51 ?  68  TYR   A OH   1 
ATOM   1589 H  H    . TYR   A 1 68  ? 37.795 5.799   3.897   1.00 15.12 ?  68  TYR   A H    1 
ATOM   1590 H  HA   . TYR   A 1 68  ? 39.415 3.829   3.459   1.00 15.13 ?  68  TYR   A HA   1 
ATOM   1591 H  HB2  . TYR   A 1 68  ? 37.369 3.316   4.363   1.00 15.66 ?  68  TYR   A HB2  1 
ATOM   1592 H  HB3  . TYR   A 1 68  ? 36.611 3.887   3.085   1.00 15.66 ?  68  TYR   A HB3  1 
ATOM   1593 H  HD1  . TYR   A 1 68  ? 36.628 2.574   0.997   1.00 19.10 ?  68  TYR   A HD1  1 
ATOM   1594 H  HD2  . TYR   A 1 68  ? 38.288 1.052   4.301   1.00 19.61 ?  68  TYR   A HD2  1 
ATOM   1595 H  HE1  . TYR   A 1 68  ? 36.718 0.526   -0.015  1.00 20.56 ?  68  TYR   A HE1  1 
ATOM   1596 H  HE2  . TYR   A 1 68  ? 38.379 -1.045  3.267   1.00 20.12 ?  68  TYR   A HE2  1 
ATOM   1597 H  HH   . TYR   A 1 68  ? 37.963 -2.235  1.427   1.00 22.20 ?  68  TYR   A HH   1 
ATOM   1598 N  N    . ILE   A 1 69  ? 38.115 4.951   0.740   1.00 12.08 ?  69  ILE   A N    1 
ATOM   1599 C  CA   . ILE   A 1 69  ? 38.254 4.939   -0.715  1.00 12.00 ?  69  ILE   A CA   1 
ATOM   1600 C  C    . ILE   A 1 69  ? 39.589 5.544   -1.142  1.00 11.92 ?  69  ILE   A C    1 
ATOM   1601 O  O    . ILE   A 1 69  ? 40.238 5.053   -2.073  1.00 12.46 ?  69  ILE   A O    1 
ATOM   1602 C  CB   . ILE   A 1 69  ? 37.056 5.645   -1.385  1.00 12.58 ?  69  ILE   A CB   1 
ATOM   1603 C  CG1  . ILE   A 1 69  ? 35.744 4.913   -1.094  1.00 13.41 ?  69  ILE   A CG1  1 
ATOM   1604 C  CG2  . ILE   A 1 69  ? 37.285 5.800   -2.894  1.00 14.14 ?  69  ILE   A CG2  1 
ATOM   1605 C  CD1  . ILE   A 1 69  ? 35.578 3.626   -1.870  1.00 14.31 ?  69  ILE   A CD1  1 
ATOM   1606 H  H    . ILE   A 1 69  ? 37.507 5.483   1.036   1.00 14.48 ?  69  ILE   A H    1 
ATOM   1607 H  HA   . ILE   A 1 69  ? 38.251 4.018   -1.009  1.00 14.39 ?  69  ILE   A HA   1 
ATOM   1608 H  HB   . ILE   A 1 69  ? 36.986 6.532   -1.008  1.00 15.08 ?  69  ILE   A HB   1 
ATOM   1609 H  HG12 . ILE   A 1 69  ? 35.711 4.694   -0.148  1.00 16.07 ?  69  ILE   A HG12 1 
ATOM   1610 H  HG13 . ILE   A 1 69  ? 35.005 5.495   -1.321  1.00 16.07 ?  69  ILE   A HG13 1 
ATOM   1611 H  HG21 . ILE   A 1 69  ? 36.439 6.012   -3.322  1.00 16.95 ?  69  ILE   A HG21 1 
ATOM   1612 H  HG22 . ILE   A 1 69  ? 37.917 6.522   -3.048  1.00 16.95 ?  69  ILE   A HG22 1 
ATOM   1613 H  HG23 . ILE   A 1 69  ? 37.635 4.971   -3.253  1.00 16.95 ?  69  ILE   A HG23 1 
ATOM   1614 H  HD11 . ILE   A 1 69  ? 34.809 3.150   -1.520  1.00 17.15 ?  69  ILE   A HD11 1 
ATOM   1615 H  HD12 . ILE   A 1 69  ? 35.436 3.838   -2.805  1.00 17.15 ?  69  ILE   A HD12 1 
ATOM   1616 H  HD13 . ILE   A 1 69  ? 36.375 3.087   -1.767  1.00 17.15 ?  69  ILE   A HD13 1 
ATOM   1617 N  N    . ALA   A 1 70  ? 40.010 6.627   -0.486  1.00 12.61 ?  70  ALA   A N    1 
ATOM   1618 C  CA   . ALA   A 1 70  ? 41.292 7.233   -0.833  1.00 13.32 ?  70  ALA   A CA   1 
ATOM   1619 C  C    . ALA   A 1 70  ? 42.435 6.244   -0.660  1.00 13.68 ?  70  ALA   A C    1 
ATOM   1620 O  O    . ALA   A 1 70  ? 43.406 6.278   -1.423  1.00 15.61 ?  70  ALA   A O    1 
ATOM   1621 C  CB   . ALA   A 1 70  ? 41.536 8.489   0.007   1.00 14.26 ?  70  ALA   A CB   1 
ATOM   1622 H  H    . ALA   A 1 70  ? 39.579 7.025   0.141   1.00 15.12 ?  70  ALA   A H    1 
ATOM   1623 H  HA   . ALA   A 1 70  ? 41.269 7.507   -1.766  1.00 15.97 ?  70  ALA   A HA   1 
ATOM   1624 H  HB1  . ALA   A 1 70  ? 42.397 8.872   -0.241  1.00 17.09 ?  70  ALA   A HB1  1 
ATOM   1625 H  HB2  . ALA   A 1 70  ? 40.832 9.131   -0.161  1.00 17.09 ?  70  ALA   A HB2  1 
ATOM   1626 H  HB3  . ALA   A 1 70  ? 41.548 8.244   0.946   1.00 17.09 ?  70  ALA   A HB3  1 
ATOM   1627 N  N    . THR   A 1 71  ? 42.328 5.345   0.317   1.00 13.34 ?  71  THR   A N    1 
ATOM   1628 C  CA   . THR   A 1 71  ? 43.379 4.365   0.572   1.00 14.72 ?  71  THR   A CA   1 
ATOM   1629 C  C    . THR   A 1 71  ? 43.262 3.141   -0.326  1.00 14.83 ?  71  THR   A C    1 
ATOM   1630 O  O    . THR   A 1 71  ? 44.277 2.624   -0.811  1.00 16.96 ?  71  THR   A O    1 
ATOM   1631 C  CB   . THR   A 1 71  ? 43.307 3.919   2.029   1.00 17.10 ?  71  THR   A CB   1 
ATOM   1632 O  OG1  . THR   A 1 71  ? 43.553 5.047   2.874   1.00 18.50 ?  71  THR   A OG1  1 
ATOM   1633 C  CG2  . THR   A 1 71  ? 44.321 2.817   2.318   1.00 18.80 ?  71  THR   A CG2  1 
ATOM   1634 H  H    . THR   A 1 71  ? 41.649 5.277   0.839   1.00 15.99 ?  71  THR   A H    1 
ATOM   1635 H  HA   . THR   A 1 71  ? 44.242 4.770   0.413   1.00 17.65 ?  71  THR   A HA   1 
ATOM   1636 H  HB   . THR   A 1 71  ? 42.419 3.560   2.204   1.00 20.50 ?  71  THR   A HB   1 
ATOM   1637 H  HG1  . THR   A 1 71  ? 42.961 5.628   2.739   1.00 22.18 ?  71  THR   A HG1  1 
ATOM   1638 H  HG21 . THR   A 1 71  ? 44.449 2.733   3.276   1.00 22.54 ?  71  THR   A HG21 1 
ATOM   1639 H  HG22 . THR   A 1 71  ? 44.011 1.967   1.968   1.00 22.54 ?  71  THR   A HG22 1 
ATOM   1640 H  HG23 . THR   A 1 71  ? 45.174 3.035   1.908   1.00 22.54 ?  71  THR   A HG23 1 
ATOM   1641 N  N    . ASN   A 1 72  ? 42.037 2.639   -0.524  1.00 13.81 ?  72  ASN   A N    1 
ATOM   1642 C  CA   . ASN   A 1 72  ? 41.820 1.311   -1.084  1.00 13.96 ?  72  ASN   A CA   1 
ATOM   1643 C  C    . ASN   A 1 72  ? 41.197 1.295   -2.468  1.00 14.21 ?  72  ASN   A C    1 
ATOM   1644 O  O    . ASN   A 1 72  ? 41.203 0.238   -3.114  1.00 15.54 ?  72  ASN   A O    1 
ATOM   1645 C  CB   . ASN   A 1 72  ? 40.923 0.498   -0.145  1.00 14.68 ?  72  ASN   A CB   1 
ATOM   1646 C  CG   . ASN   A 1 72  ? 41.537 0.337   1.219   1.00 15.93 ?  72  ASN   A CG   1 
ATOM   1647 O  OD1  . ASN   A 1 72  ? 41.086 0.934   2.194   1.00 17.67 ?  72  ASN   A OD1  1 
ATOM   1648 N  ND2  . ASN   A 1 72  ? 42.589 -0.448  1.292   1.00 16.66 ?  72  ASN   A ND2  1 
ATOM   1649 H  H    . ASN   A 1 72  ? 41.304 3.057   -0.340  1.00 16.55 ?  72  ASN   A H    1 
ATOM   1650 H  HA   . ASN   A 1 72  ? 42.674 0.859   -1.147  1.00 16.74 ?  72  ASN   A HA   1 
ATOM   1651 H  HB2  . ASN   A 1 72  ? 40.071 0.948   -0.051  1.00 17.60 ?  72  ASN   A HB2  1 
ATOM   1652 H  HB3  . ASN   A 1 72  ? 40.792 -0.388  -0.525  1.00 17.60 ?  72  ASN   A HB3  1 
ATOM   1653 H  HD21 . ASN   A 1 72  ? 42.976 -0.567  2.049   1.00 19.97 ?  72  ASN   A HD21 1 
ATOM   1654 H  HD22 . ASN   A 1 72  ? 42.884 -0.838  0.587   1.00 19.97 ?  72  ASN   A HD22 1 
ATOM   1655 N  N    . GLY   A 1 73  ? 40.646 2.409   -2.932  1.00 13.95 ?  73  GLY   A N    1 
ATOM   1656 C  CA   . GLY   A 1 73  ? 39.916 2.419   -4.174  1.00 13.53 ?  73  GLY   A CA   1 
ATOM   1657 C  C    . GLY   A 1 73  ? 38.519 1.848   -4.008  1.00 12.92 ?  73  GLY   A C    1 
ATOM   1658 O  O    . GLY   A 1 73  ? 38.126 1.394   -2.926  1.00 13.63 ?  73  GLY   A O    1 
ATOM   1659 H  H    . GLY   A 1 73  ? 40.687 3.183   -2.544  1.00 16.73 ?  73  GLY   A H    1 
ATOM   1660 H  HA2  . GLY   A 1 73  ? 39.843 3.335   -4.500  1.00 16.22 ?  73  GLY   A HA2  1 
ATOM   1661 H  HA3  . GLY   A 1 73  ? 40.392 1.897   -4.838  1.00 16.22 ?  73  GLY   A HA3  1 
ATOM   1662 N  N    . PRO   A 1 74  ? 37.747 1.861   -5.093  1.00 13.60 ?  74  PRO   A N    1 
ATOM   1663 C  CA   . PRO   A 1 74  ? 36.349 1.429   -5.017  1.00 13.71 ?  74  PRO   A CA   1 
ATOM   1664 C  C    . PRO   A 1 74  ? 36.201 -0.051  -4.693  1.00 12.71 ?  74  PRO   A C    1 
ATOM   1665 O  O    . PRO   A 1 74  ? 37.071 -0.879  -4.981  1.00 13.68 ?  74  PRO   A O    1 
ATOM   1666 C  CB   . PRO   A 1 74  ? 35.809 1.724   -6.423  1.00 15.60 ?  74  PRO   A CB   1 
ATOM   1667 C  CG   . PRO   A 1 74  ? 36.768 2.697   -7.029  1.00 18.35 ?  74  PRO   A CG   1 
ATOM   1668 C  CD   . PRO   A 1 74  ? 38.099 2.374   -6.428  1.00 15.54 ?  74  PRO   A CD   1 
ATOM   1669 H  HA   . PRO   A 1 74  ? 35.865 1.961   -4.365  1.00 16.44 ?  74  PRO   A HA   1 
ATOM   1670 H  HB2  . PRO   A 1 74  ? 35.783 0.902   -6.937  1.00 18.70 ?  74  PRO   A HB2  1 
ATOM   1671 H  HB3  . PRO   A 1 74  ? 34.924 2.114   -6.356  1.00 18.70 ?  74  PRO   A HB3  1 
ATOM   1672 H  HG2  . PRO   A 1 74  ? 36.792 2.578   -7.991  1.00 22.00 ?  74  PRO   A HG2  1 
ATOM   1673 H  HG3  . PRO   A 1 74  ? 36.506 3.601   -6.802  1.00 22.00 ?  74  PRO   A HG3  1 
ATOM   1674 H  HD2  . PRO   A 1 74  ? 38.552 1.688   -6.950  1.00 18.63 ?  74  PRO   A HD2  1 
ATOM   1675 H  HD3  . PRO   A 1 74  ? 38.641 3.179   -6.365  1.00 18.63 ?  74  PRO   A HD3  1 
ATOM   1676 N  N    . LEU   A 1 75  ? 35.055 -0.372  -4.101  1.00 12.06 ?  75  LEU   A N    1 
ATOM   1677 C  CA   . LEU   A 1 75  ? 34.647 -1.759  -3.950  1.00 11.68 ?  75  LEU   A CA   1 
ATOM   1678 C  C    . LEU   A 1 75  ? 34.263 -2.338  -5.309  1.00 12.29 ?  75  LEU   A C    1 
ATOM   1679 O  O    . LEU   A 1 75  ? 34.139 -1.624  -6.310  1.00 13.52 ?  75  LEU   A O    1 
ATOM   1680 C  CB   . LEU   A 1 75  ? 33.458 -1.871  -2.995  1.00 11.83 ?  75  LEU   A CB   1 
ATOM   1681 C  CG   . LEU   A 1 75  ? 33.667 -1.462  -1.540  1.00 13.55 ?  75  LEU   A CG   1 
ATOM   1682 C  CD1  . LEU   A 1 75  ? 32.388 -1.677  -0.743  1.00 15.50 ?  75  LEU   A CD1  1 
ATOM   1683 C  CD2  . LEU   A 1 75  ? 34.813 -2.184  -0.886  1.00 16.83 ?  75  LEU   A CD2  1 
ATOM   1684 H  H    . LEU   A 1 75  ? 34.498 0.200   -3.782  1.00 14.46 ?  75  LEU   A H    1 
ATOM   1685 H  HA   . LEU   A 1 75  ? 35.385 -2.272  -3.595  1.00 14.00 ?  75  LEU   A HA   1 
ATOM   1686 H  HB2  . LEU   A 1 75  ? 32.740 -1.325  -3.343  1.00 14.18 ?  75  LEU   A HB2  1 
ATOM   1687 H  HB3  . LEU   A 1 75  ? 33.175 -2.801  -2.988  1.00 14.18 ?  75  LEU   A HB3  1 
ATOM   1688 H  HG   . LEU   A 1 75  ? 33.874 -0.513  -1.514  1.00 16.25 ?  75  LEU   A HG   1 
ATOM   1689 H  HD11 . LEU   A 1 75  ? 32.541 -1.406  0.176   1.00 18.59 ?  75  LEU   A HD11 1 
ATOM   1690 H  HD12 . LEU   A 1 75  ? 31.684 -1.138  -1.135  1.00 18.59 ?  75  LEU   A HD12 1 
ATOM   1691 H  HD13 . LEU   A 1 75  ? 32.151 -2.614  -0.780  1.00 18.59 ?  75  LEU   A HD13 1 
ATOM   1692 H  HD21 . LEU   A 1 75  ? 34.864 -1.921  0.047   1.00 20.18 ?  75  LEU   A HD21 1 
ATOM   1693 H  HD22 . LEU   A 1 75  ? 34.669 -3.138  -0.956  1.00 20.18 ?  75  LEU   A HD22 1 
ATOM   1694 H  HD23 . LEU   A 1 75  ? 35.642 -1.941  -1.338  1.00 20.18 ?  75  LEU   A HD23 1 
ATOM   1695 N  N    . LYS   A 1 76  ? 34.078 -3.657  -5.329  1.00 12.61 ?  76  LYS   A N    1 
ATOM   1696 C  CA   . LYS   A 1 76  ? 33.482 -4.370  -6.453  1.00 13.28 ?  76  LYS   A CA   1 
ATOM   1697 C  C    . LYS   A 1 76  ? 31.969 -4.456  -6.260  1.00 11.84 ?  76  LYS   A C    1 
ATOM   1698 O  O    . LYS   A 1 76  ? 31.485 -4.567  -5.136  1.00 12.12 ?  76  LYS   A O    1 
ATOM   1699 C  CB   . LYS   A 1 76  ? 34.027 -5.807  -6.514  1.00 14.82 ?  76  LYS   A CB   1 
ATOM   1700 C  CG   . LYS   A 1 76  ? 35.534 -5.913  -6.697  1.00 16.32 ?  76  LYS   A CG   1 
ATOM   1701 C  CD   . LYS   A 1 76  ? 36.045 -7.322  -6.509  1.00 17.72 ?  76  LYS   A CD   1 
ATOM   1702 C  CE   . LYS   A 1 76  ? 37.547 -7.380  -6.683  1.00 20.16 ?  76  LYS   A CE   1 
ATOM   1703 N  NZ   . LYS   A 1 76  ? 38.072 -8.744  -6.483  1.00 20.97 ?  76  LYS   A NZ   1 
ATOM   1704 H  H    . LYS   A 1 76  ? 34.299 -4.176  -4.676  1.00 15.12 ?  76  LYS   A H    1 
ATOM   1705 H  HA   . LYS   A 1 76  ? 33.681 -3.912  -7.285  1.00 15.92 ?  76  LYS   A HA   1 
ATOM   1706 H  HB2  . LYS   A 1 76  ? 33.801 -6.256  -5.687  1.00 17.77 ?  76  LYS   A HB2  1 
ATOM   1707 H  HB3  . LYS   A 1 76  ? 33.609 -6.260  -7.260  1.00 17.77 ?  76  LYS   A HB3  1 
ATOM   1708 H  HG2  . LYS   A 1 76  ? 35.766 -5.624  -7.595  1.00 19.57 ?  76  LYS   A HG2  1 
ATOM   1709 H  HG3  . LYS   A 1 76  ? 35.975 -5.344  -6.044  1.00 19.57 ?  76  LYS   A HG3  1 
ATOM   1710 H  HD2  . LYS   A 1 76  ? 35.825 -7.628  -5.615  1.00 21.24 ?  76  LYS   A HD2  1 
ATOM   1711 H  HD3  . LYS   A 1 76  ? 35.637 -7.902  -7.173  1.00 21.24 ?  76  LYS   A HD3  1 
ATOM   1712 H  HE2  . LYS   A 1 76  ? 37.776 -7.094  -7.580  1.00 24.18 ?  76  LYS   A HE2  1 
ATOM   1713 H  HE3  . LYS   A 1 76  ? 37.964 -6.798  -6.028  1.00 24.18 ?  76  LYS   A HE3  1 
ATOM   1714 H  HZ1  . LYS   A 1 76  ? 38.955 -8.758  -6.590  1.00 25.15 ?  76  LYS   A HZ1  1 
ATOM   1715 H  HZ2  . LYS   A 1 76  ? 37.877 -9.036  -5.663  1.00 25.15 ?  76  LYS   A HZ2  1 
ATOM   1716 H  HZ3  . LYS   A 1 76  ? 37.705 -9.306  -7.076  1.00 25.15 ?  76  LYS   A HZ3  1 
ATOM   1717 N  N    . VAL   A 1 77  ? 31.218 -4.424  -7.366  1.00 12.40 ?  77  VAL   A N    1 
ATOM   1718 C  CA   . VAL   A 1 77  ? 29.809 -4.811  -7.284  1.00 12.22 ?  77  VAL   A CA   1 
ATOM   1719 C  C    . VAL   A 1 77  ? 29.744 -6.266  -6.840  1.00 12.00 ?  77  VAL   A C    1 
ATOM   1720 O  O    . VAL   A 1 77  ? 30.405 -7.137  -7.419  1.00 12.41 ?  77  VAL   A O    1 
ATOM   1721 C  CB   . VAL   A 1 77  ? 29.085 -4.590  -8.621  1.00 13.19 ?  77  VAL   A CB   1 
ATOM   1722 C  CG1  . VAL   A 1 77  ? 27.625 -5.021  -8.509  1.00 14.03 ?  77  VAL   A CG1  1 
ATOM   1723 C  CG2  . VAL   A 1 77  ? 29.182 -3.136  -9.045  1.00 14.63 ?  77  VAL   A CG2  1 
ATOM   1724 H  H    . VAL   A 1 77  ? 31.498 -4.187  -8.144  1.00 14.87 ?  77  VAL   A H    1 
ATOM   1725 H  HA   . VAL   A 1 77  ? 29.376 -4.271  -6.609  1.00 14.65 ?  77  VAL   A HA   1 
ATOM   1726 H  HB   . VAL   A 1 77  ? 29.511 -5.130  -9.304  1.00 15.81 ?  77  VAL   A HB   1 
ATOM   1727 H  HG11 . VAL   A 1 77  ? 27.150 -4.715  -9.295  1.00 16.82 ?  77  VAL   A HG11 1 
ATOM   1728 H  HG12 . VAL   A 1 77  ? 27.585 -5.987  -8.450  1.00 16.82 ?  77  VAL   A HG12 1 
ATOM   1729 H  HG13 . VAL   A 1 77  ? 27.241 -4.622  -7.712  1.00 16.82 ?  77  VAL   A HG13 1 
ATOM   1730 H  HG21 . VAL   A 1 77  ? 28.670 -3.014  -9.858  1.00 17.54 ?  77  VAL   A HG21 1 
ATOM   1731 H  HG22 . VAL   A 1 77  ? 28.821 -2.578  -8.338  1.00 17.54 ?  77  VAL   A HG22 1 
ATOM   1732 H  HG23 . VAL   A 1 77  ? 30.112 -2.912  -9.201  1.00 17.54 ?  77  VAL   A HG23 1 
ATOM   1733 N  N    . GLY   A 1 78  ? 28.958 -6.535  -5.797  1.00 11.72 ?  78  GLY   A N    1 
ATOM   1734 C  CA   . GLY   A 1 78  ? 28.941 -7.823  -5.138  1.00 11.94 ?  78  GLY   A CA   1 
ATOM   1735 C  C    . GLY   A 1 78  ? 29.853 -7.909  -3.936  1.00 11.39 ?  78  GLY   A C    1 
ATOM   1736 O  O    . GLY   A 1 78  ? 29.795 -8.911  -3.208  1.00 12.14 ?  78  GLY   A O    1 
ATOM   1737 H  H    . GLY   A 1 78  ? 28.410 -5.960  -5.454  1.00 14.05 ?  78  GLY   A H    1 
ATOM   1738 H  HA2  . GLY   A 1 78  ? 28.037 -8.014  -4.851  1.00 14.32 ?  78  GLY   A HA2  1 
ATOM   1739 H  HA3  . GLY   A 1 78  ? 29.209 -8.502  -5.776  1.00 14.32 ?  78  GLY   A HA3  1 
ATOM   1740 N  N    . GLY   A 1 79  ? 30.709 -6.907  -3.714  1.00 11.39 ?  79  GLY   A N    1 
ATOM   1741 C  CA   . GLY   A 1 79  ? 31.664 -6.928  -2.630  1.00 11.88 ?  79  GLY   A CA   1 
ATOM   1742 C  C    . GLY   A 1 79  ? 31.216 -6.128  -1.420  1.00 11.10 ?  79  GLY   A C    1 
ATOM   1743 O  O    . GLY   A 1 79  ? 30.099 -5.612  -1.347  1.00 11.75 ?  79  GLY   A O    1 
ATOM   1744 H  H    . GLY   A 1 79  ? 30.752 -6.195  -4.196  1.00 13.66 ?  79  GLY   A H    1 
ATOM   1745 H  HA2  . GLY   A 1 79  ? 31.812 -7.852  -2.356  1.00 14.24 ?  79  GLY   A HA2  1 
ATOM   1746 H  HA3  . GLY   A 1 79  ? 32.508 -6.570  -2.942  1.00 14.24 ?  79  GLY   A HA3  1 
ATOM   1747 N  N    . SER   A 1 80  ? 32.121 -6.029  -0.448  1.00 11.75 ?  80  SER   A N    1 
ATOM   1748 C  CA   . SER   A 1 80  ? 31.799 -5.397  0.820   1.00 11.36 ?  80  SER   A CA   1 
ATOM   1749 C  C    . SER   A 1 80  ? 33.071 -4.953  1.525   1.00 11.22 ?  80  SER   A C    1 
ATOM   1750 O  O    . SER   A 1 80  ? 34.182 -5.387  1.200   1.00 12.96 ?  80  SER   A O    1 
ATOM   1751 C  CB   . SER   A 1 80  ? 31.034 -6.355  1.738   1.00 12.33 ?  80  SER   A CB   1 
ATOM   1752 O  OG   . SER   A 1 80  ? 31.867 -7.408  2.210   1.00 14.04 ?  80  SER   A OG   1 
ATOM   1753 H  H    . SER   A 1 80  ? 32.932 -6.314  -0.506  1.00 14.08 ?  80  SER   A H    1 
ATOM   1754 H  HA   . SER   A 1 80  ? 31.249 -4.610  0.638   1.00 13.61 ?  80  SER   A HA   1 
ATOM   1755 H  HB2  . SER   A 1 80  ? 30.698 -5.849  2.493   1.00 14.78 ?  80  SER   A HB2  1 
ATOM   1756 H  HB3  . SER   A 1 80  ? 30.291 -6.729  1.237   1.00 14.78 ?  80  SER   A HB3  1 
ATOM   1757 H  HG   . SER   A 1 80  ? 32.160 -7.842  1.551   1.00 16.83 ?  80  SER   A HG   1 
ATOM   1758 N  N    . CYS   A 1 81  ? 32.881 -4.098  2.527   1.00 11.01 ?  81  CYS   A N    1 
ATOM   1759 C  CA   . CYS   A 1 81  ? 33.932 -3.816  3.491   1.00 11.28 ?  81  CYS   A CA   1 
ATOM   1760 C  C    . CYS   A 1 81  ? 33.286 -3.579  4.849   1.00 11.14 ?  81  CYS   A C    1 
ATOM   1761 O  O    . CYS   A 1 81  ? 32.118 -3.178  4.937   1.00 12.39 ?  81  CYS   A O    1 
ATOM   1762 C  CB   . CYS   A 1 81  ? 34.805 -2.622  3.078   1.00 11.93 ?  81  CYS   A CB   1 
ATOM   1763 S  SG   . CYS   A 1 81  ? 33.909 -1.046  3.086   1.00 12.10 ?  81  CYS   A SG   1 
ATOM   1764 H  H    . CYS   A 1 81  ? 32.146 -3.672  2.674   1.00 13.19 ?  81  CYS   A H    1 
ATOM   1765 H  HA   . CYS   A 1 81  ? 34.508 -4.591  3.564   1.00 13.52 ?  81  CYS   A HA   1 
ATOM   1766 H  HB2  . CYS   A 1 81  ? 35.554 -2.550  3.695   1.00 14.30 ?  81  CYS   A HB2  1 
ATOM   1767 H  HB3  . CYS   A 1 81  ? 35.142 -2.774  2.177   1.00 14.30 ?  81  CYS   A HB3  1 
ATOM   1768 H  HG   . CYS   A 1 81  ? 34.658 -0.167  2.756   1.00 14.50 ?  81  CYS   A HG   1 
ATOM   1769 N  N    . VAL   A 1 82  ? 34.056 -3.836  5.905   1.00 11.56 ?  82  VAL   A N    1 
ATOM   1770 C  CA   . VAL   A 1 82  ? 33.628 -3.592  7.277   1.00 11.98 ?  82  VAL   A CA   1 
ATOM   1771 C  C    . VAL   A 1 82  ? 34.225 -2.276  7.748   1.00 12.18 ?  82  VAL   A C    1 
ATOM   1772 O  O    . VAL   A 1 82  ? 35.449 -2.103  7.737   1.00 12.92 ?  82  VAL   A O    1 
ATOM   1773 C  CB   . VAL   A 1 82  ? 34.048 -4.734  8.212   1.00 13.58 ?  82  VAL   A CB   1 
ATOM   1774 C  CG1  . VAL   A 1 82  ? 33.595 -4.438  9.633   1.00 14.86 ?  82  VAL   A CG1  1 
ATOM   1775 C  CG2  . VAL   A 1 82  ? 33.481 -6.060  7.734   1.00 14.63 ?  82  VAL   A CG2  1 
ATOM   1776 H  H    . VAL   A 1 82  ? 34.852 -4.170  5.849   1.00 13.85 ?  82  VAL   A H    1 
ATOM   1777 H  HA   . VAL   A 1 82  ? 32.661 -3.510  7.298   1.00 14.36 ?  82  VAL   A HA   1 
ATOM   1778 H  HB   . VAL   A 1 82  ? 35.012 -4.797  8.213   1.00 16.28 ?  82  VAL   A HB   1 
ATOM   1779 H  HG11 . VAL   A 1 82  ? 33.681 -5.246  10.162  1.00 17.82 ?  82  VAL   A HG11 1 
ATOM   1780 H  HG12 . VAL   A 1 82  ? 34.152 -3.737  10.008  1.00 17.82 ?  82  VAL   A HG12 1 
ATOM   1781 H  HG13 . VAL   A 1 82  ? 32.667 -4.151  9.619   1.00 17.82 ?  82  VAL   A HG13 1 
ATOM   1782 H  HG21 . VAL   A 1 82  ? 33.723 -6.752  8.367   1.00 17.54 ?  82  VAL   A HG21 1 
ATOM   1783 H  HG22 . VAL   A 1 82  ? 32.513 -5.990  7.675   1.00 17.54 ?  82  VAL   A HG22 1 
ATOM   1784 H  HG23 . VAL   A 1 82  ? 33.849 -6.265  6.860   1.00 17.54 ?  82  VAL   A HG23 1 
ATOM   1785 N  N    . LEU   A 1 83  ? 33.367 -1.348  8.160   1.00 11.72 ?  83  LEU   A N    1 
ATOM   1786 C  CA   . LEU   A 1 83  ? 33.790 -0.085  8.743   1.00 11.45 ?  83  LEU   A CA   1 
ATOM   1787 C  C    . LEU   A 1 83  ? 33.071 0.097   10.077  1.00 11.80 ?  83  LEU   A C    1 
ATOM   1788 O  O    . LEU   A 1 83  ? 32.351 -0.794  10.544  1.00 12.35 ?  83  LEU   A O    1 
ATOM   1789 C  CB   . LEU   A 1 83  ? 33.546 1.074   7.765   1.00 11.94 ?  83  LEU   A CB   1 
ATOM   1790 C  CG   . LEU   A 1 83  ? 34.447 1.072   6.527   1.00 12.76 ?  83  LEU   A CG   1 
ATOM   1791 C  CD1  . LEU   A 1 83  ? 34.016 2.126   5.531   1.00 13.16 ?  83  LEU   A CD1  1 
ATOM   1792 C  CD2  . LEU   A 1 83  ? 35.917 1.277   6.912   1.00 13.11 ?  83  LEU   A CD2  1 
ATOM   1793 H  H    . LEU   A 1 83  ? 32.511 -1.428  8.105   1.00 14.05 ?  83  LEU   A H    1 
ATOM   1794 H  HA   . LEU   A 1 83  ? 34.739 -0.115  8.920   1.00 13.72 ?  83  LEU   A HA   1 
ATOM   1795 H  HB2  . LEU   A 1 83  ? 32.628 1.036   7.450   1.00 14.31 ?  83  LEU   A HB2  1 
ATOM   1796 H  HB3  . LEU   A 1 83  ? 33.692 1.915   8.226   1.00 14.31 ?  83  LEU   A HB3  1 
ATOM   1797 H  HG   . LEU   A 1 83  ? 34.376 0.213   6.089   1.00 15.29 ?  83  LEU   A HG   1 
ATOM   1798 H  HD11 . LEU   A 1 83  ? 34.608 2.091   4.759   1.00 15.78 ?  83  LEU   A HD11 1 
ATOM   1799 H  HD12 . LEU   A 1 83  ? 33.106 1.946   5.256   1.00 15.78 ?  83  LEU   A HD12 1 
ATOM   1800 H  HD13 . LEU   A 1 83  ? 34.073 2.999   5.948   1.00 15.78 ?  83  LEU   A HD13 1 
ATOM   1801 H  HD21 . LEU   A 1 83  ? 36.440 1.436   6.108   1.00 15.72 ?  83  LEU   A HD21 1 
ATOM   1802 H  HD22 . LEU   A 1 83  ? 35.989 2.042   7.505   1.00 15.72 ?  83  LEU   A HD22 1 
ATOM   1803 H  HD23 . LEU   A 1 83  ? 36.242 0.481   7.361   1.00 15.72 ?  83  LEU   A HD23 1 
ATOM   1804 N  N    . SER   A 1 84  ? 33.280 1.247   10.709  1.00 12.25 ?  84  SER   A N    1 
ATOM   1805 C  CA   . SER   A 1 84  ? 32.635 1.509   11.986  1.00 12.48 ?  84  SER   A CA   1 
ATOM   1806 C  C    . SER   A 1 84  ? 31.116 1.596   11.837  1.00 12.32 ?  84  SER   A C    1 
ATOM   1807 O  O    . SER   A 1 84  ? 30.590 2.052   10.822  1.00 12.52 ?  84  SER   A O    1 
ATOM   1808 C  CB   . SER   A 1 84  ? 33.126 2.836   12.554  1.00 13.28 ?  84  SER   A CB   1 
ATOM   1809 O  OG   . SER   A 1 84  ? 32.500 3.107   13.790  1.00 14.21 ?  84  SER   A OG   1 
ATOM   1810 H  H    . SER   A 1 84  ? 33.781 1.893   10.416  1.00 14.69 ?  84  SER   A H    1 
ATOM   1811 H  HA   . SER   A 1 84  ? 32.859 0.800   12.607  1.00 14.95 ?  84  SER   A HA   1 
ATOM   1812 H  HB2  . SER   A 1 84  ? 34.087 2.793   12.681  1.00 15.92 ?  84  SER   A HB2  1 
ATOM   1813 H  HB3  . SER   A 1 84  ? 32.907 3.547   11.930  1.00 15.92 ?  84  SER   A HB3  1 
ATOM   1814 H  HG   . SER   A 1 84  ? 32.779 3.833   14.103  1.00 17.03 ?  84  SER   A HG   1 
ATOM   1815 N  N    . GLY   A 1 85  ? 30.407 1.180   12.885  1.00 13.29 ?  85  GLY   A N    1 
ATOM   1816 C  CA   . GLY   A 1 85  ? 28.983 1.418   12.965  1.00 13.83 ?  85  GLY   A CA   1 
ATOM   1817 C  C    . GLY   A 1 85  ? 28.615 2.736   13.604  1.00 13.42 ?  85  GLY   A C    1 
ATOM   1818 O  O    . GLY   A 1 85  ? 27.424 3.048   13.717  1.00 13.91 ?  85  GLY   A O    1 
ATOM   1819 H  H    . GLY   A 1 85  ? 30.738 0.757   13.561  1.00 15.93 ?  85  GLY   A H    1 
ATOM   1820 H  HA2  . GLY   A 1 85  ? 28.611 1.397   12.070  1.00 16.58 ?  85  GLY   A HA2  1 
ATOM   1821 H  HA3  . GLY   A 1 85  ? 28.574 0.707   13.479  1.00 16.58 ?  85  GLY   A HA3  1 
ATOM   1822 N  N    . HIS   A 1 86  ? 29.602 3.510   14.048  1.00 13.14 ?  86  HIS   A N    1 
ATOM   1823 C  CA   . HIS   A 1 86  ? 29.379 4.848   14.615  1.00 13.85 ?  86  HIS   A CA   1 
ATOM   1824 C  C    . HIS   A 1 86  ? 28.386 4.729   15.765  1.00 14.44 ?  86  HIS   A C    1 
ATOM   1825 O  O    . HIS   A 1 86  ? 28.562 3.849   16.623  1.00 15.70 ?  86  HIS   A O    1 
ATOM   1826 C  CB   . HIS   A 1 86  ? 29.011 5.823   13.505  1.00 13.69 ?  86  HIS   A CB   1 
ATOM   1827 C  CG   . HIS   A 1 86  ? 30.072 5.920   12.468  1.00 13.38 ?  86  HIS   A CG   1 
ATOM   1828 N  ND1  . HIS   A 1 86  ? 31.160 6.756   12.600  1.00 14.59 ?  86  HIS   A ND1  1 
ATOM   1829 C  CD2  . HIS   A 1 86  ? 30.254 5.233   11.318  1.00 13.23 ?  86  HIS   A CD2  1 
ATOM   1830 C  CE1  . HIS   A 1 86  ? 31.954 6.595   11.558  1.00 14.40 ?  86  HIS   A CE1  1 
ATOM   1831 N  NE2  . HIS   A 1 86  ? 31.433 5.671   10.772  1.00 13.86 ?  86  HIS   A NE2  1 
ATOM   1832 H  H    . HIS   A 1 86  ? 30.425 3.281   14.047  1.00 15.76 ?  86  HIS   A H    1 
ATOM   1833 H  HA   . HIS   A 1 86  ? 30.214 5.159   14.991  1.00 16.60 ?  86  HIS   A HA   1 
ATOM   1834 H  HB2  . HIS   A 1 86  ? 28.190 5.529   13.074  1.00 16.42 ?  86  HIS   A HB2  1 
ATOM   1835 H  HB3  . HIS   A 1 86  ? 28.881 6.711   13.883  1.00 16.42 ?  86  HIS   A HB3  1 
ATOM   1836 H  HD2  . HIS   A 1 86  ? 29.691 4.575   10.967  1.00 15.86 ?  86  HIS   A HD2  1 
ATOM   1837 H  HE1  . HIS   A 1 86  ? 32.746 7.053   11.395  1.00 17.26 ?  86  HIS   A HE1  1 
ATOM   1838 H  HE2  . HIS   A 1 86  ? 31.771 5.395   10.022  1.00 16.62 ?  86  HIS   A HE2  1 
ATOM   1839 N  N    . ASN   A 1 87  ? 27.375 5.584   15.833  1.00 15.24 ?  87  ASN   A N    1 
ATOM   1840 C  CA   . ASN   A 1 87  ? 26.392 5.571   16.900  1.00 16.13 ?  87  ASN   A CA   1 
ATOM   1841 C  C    . ASN   A 1 87  ? 25.270 4.576   16.658  1.00 17.23 ?  87  ASN   A C    1 
ATOM   1842 O  O    . ASN   A 1 87  ? 24.346 4.511   17.471  1.00 19.59 ?  87  ASN   A O    1 
ATOM   1843 C  CB   . ASN   A 1 87  ? 25.793 6.975   17.061  1.00 17.44 ?  87  ASN   A CB   1 
ATOM   1844 C  CG   . ASN   A 1 87  ? 25.299 7.561   15.741  1.00 18.36 ?  87  ASN   A CG   1 
ATOM   1845 O  OD1  . ASN   A 1 87  ? 25.945 7.432   14.702  1.00 18.74 ?  87  ASN   A OD1  1 
ATOM   1846 N  ND2  . ASN   A 1 87  ? 24.152 8.211   15.782  1.00 19.26 ?  87  ASN   A ND2  1 
ATOM   1847 H  H    . ASN   A 1 87  ? 27.233 6.202   15.255  1.00 18.27 ?  87  ASN   A H    1 
ATOM   1848 H  HA   . ASN   A 1 87  ? 26.822 5.329   17.741  1.00 19.34 ?  87  ASN   A HA   1 
ATOM   1849 H  HB2  . ASN   A 1 87  ? 25.035 6.927   17.675  1.00 20.91 ?  87  ASN   A HB2  1 
ATOM   1850 H  HB3  . ASN   A 1 87  ? 26.468 7.567   17.422  1.00 20.91 ?  87  ASN   A HB3  1 
ATOM   1851 H  HD21 . ASN   A 1 87  ? 23.836 8.554   15.062  1.00 23.10 ?  87  ASN   A HD21 1 
ATOM   1852 H  HD22 . ASN   A 1 87  ? 23.730 8.295   16.525  1.00 23.10 ?  87  ASN   A HD22 1 
ATOM   1853 N  N    . LEU   A 1 88  ? 25.329 3.799   15.583  1.00 16.11 ?  88  LEU   A N    1 
ATOM   1854 C  CA   . LEU   A 1 88  ? 24.213 2.947   15.188  1.00 16.19 ?  88  LEU   A CA   1 
ATOM   1855 C  C    . LEU   A 1 88  ? 24.419 1.468   15.488  1.00 15.82 ?  88  LEU   A C    1 
ATOM   1856 O  O    . LEU   A 1 88  ? 23.435 0.739   15.653  1.00 16.79 ?  88  LEU   A O    1 
ATOM   1857 C  CB   . LEU   A 1 88  ? 23.965 3.096   13.688  1.00 16.54 ?  88  LEU   A CB   1 
ATOM   1858 C  CG   . LEU   A 1 88  ? 23.667 4.513   13.192  1.00 18.24 ?  88  LEU   A CG   1 
ATOM   1859 C  CD1  . LEU   A 1 88  ? 23.525 4.516   11.683  1.00 18.60 ?  88  LEU   A CD1  1 
ATOM   1860 C  CD2  . LEU   A 1 88  ? 22.412 5.076   13.854  1.00 19.78 ?  88  LEU   A CD2  1 
ATOM   1861 H  H    . LEU   A 1 88  ? 26.015 3.745   15.068  1.00 19.31 ?  88  LEU   A H    1 
ATOM   1862 H  HA   . LEU   A 1 88  ? 23.416 3.240   15.653  1.00 19.41 ?  88  LEU   A HA   1 
ATOM   1863 H  HB2  . LEU   A 1 88  ? 24.750 2.789   13.214  1.00 19.84 ?  88  LEU   A HB2  1 
ATOM   1864 H  HB3  . LEU   A 1 88  ? 23.204 2.544   13.451  1.00 19.84 ?  88  LEU   A HB3  1 
ATOM   1865 H  HG   . LEU   A 1 88  ? 24.407 5.094   13.420  1.00 21.87 ?  88  LEU   A HG   1 
ATOM   1866 H  HD11 . LEU   A 1 88  ? 23.335 5.419   11.382  1.00 22.31 ?  88  LEU   A HD11 1 
ATOM   1867 H  HD12 . LEU   A 1 88  ? 24.354 4.204   11.288  1.00 22.31 ?  88  LEU   A HD12 1 
ATOM   1868 H  HD13 . LEU   A 1 88  ? 22.796 3.925   11.431  1.00 22.31 ?  88  LEU   A HD13 1 
ATOM   1869 H  HD21 . LEU   A 1 88  ? 22.193 5.927   13.443  1.00 23.72 ?  88  LEU   A HD21 1 
ATOM   1870 H  HD22 . LEU   A 1 88  ? 21.683 4.450   13.728  1.00 23.72 ?  88  LEU   A HD22 1 
ATOM   1871 H  HD23 . LEU   A 1 88  ? 22.585 5.200   14.799  1.00 23.72 ?  88  LEU   A HD23 1 
ATOM   1872 N  N    . ALA   A 1 89  ? 25.665 1.013   15.534  1.00 15.07 ?  89  ALA   A N    1 
ATOM   1873 C  CA   . ALA   A 1 89  ? 26.003 -0.399  15.637  1.00 14.91 ?  89  ALA   A CA   1 
ATOM   1874 C  C    . ALA   A 1 89  ? 27.487 -0.466  15.957  1.00 15.07 ?  89  ALA   A C    1 
ATOM   1875 O  O    . ALA   A 1 89  ? 28.203 0.530   15.839  1.00 15.78 ?  89  ALA   A O    1 
ATOM   1876 C  CB   . ALA   A 1 89  ? 25.733 -1.114  14.315  1.00 14.50 ?  89  ALA   A CB   1 
ATOM   1877 H  H    . ALA   A 1 89  ? 26.354 1.524   15.494  1.00 18.07 ?  89  ALA   A H    1 
ATOM   1878 H  HA   . ALA   A 1 89  ? 25.492 -0.819  16.348  1.00 17.88 ?  89  ALA   A HA   1 
ATOM   1879 H  HB1  . ALA   A 1 89  ? 25.979 -2.049  14.406  1.00 17.38 ?  89  ALA   A HB1  1 
ATOM   1880 H  HB2  . ALA   A 1 89  ? 24.789 -1.042  14.100  1.00 17.38 ?  89  ALA   A HB2  1 
ATOM   1881 H  HB3  . ALA   A 1 89  ? 26.264 -0.701  13.617  1.00 17.38 ?  89  ALA   A HB3  1 
ATOM   1882 N  N    . LYS   A 1 90  ? 27.959 -1.645  16.352  1.00 15.97 ?  90  LYS   A N    1 
ATOM   1883 C  CA   . LYS   A 1 90  ? 29.401 -1.798  16.506  1.00 16.83 ?  90  LYS   A CA   1 
ATOM   1884 C  C    . LYS   A 1 90  ? 30.108 -1.616  15.165  1.00 15.54 ?  90  LYS   A C    1 
ATOM   1885 O  O    . LYS   A 1 90  ? 31.048 -0.812  15.040  1.00 16.92 ?  90  LYS   A O    1 
ATOM   1886 C  CB   . LYS   A 1 90  ? 29.734 -3.156  17.127  1.00 19.79 ?  90  LYS   A CB   1 
ATOM   1887 C  CG   . LYS   A 1 90  ? 31.214 -3.319  17.453  1.00 24.85 ?  90  LYS   A CG   1 
ATOM   1888 C  CD   . LYS   A 1 90  ? 31.456 -4.544  18.321  1.00 30.64 ?  90  LYS   A CD   1 
ATOM   1889 C  CE   . LYS   A 1 90  ? 32.859 -4.547  18.914  1.00 34.89 ?  90  LYS   A CE   1 
ATOM   1890 N  NZ   . LYS   A 1 90  ? 33.909 -4.888  17.914  1.00 37.74 ?  90  LYS   A NZ   1 
ATOM   1891 H  H    . LYS   A 1 90  ? 27.483 -2.336  16.535  1.00 19.15 ?  90  LYS   A H    1 
ATOM   1892 H  HA   . LYS   A 1 90  ? 29.725 -1.110  17.107  1.00 20.18 ?  90  LYS   A HA   1 
ATOM   1893 H  HB2  . LYS   A 1 90  ? 29.231 -3.256  17.953  1.00 23.73 ?  90  LYS   A HB2  1 
ATOM   1894 H  HB3  . LYS   A 1 90  ? 29.484 -3.857  16.505  1.00 23.73 ?  90  LYS   A HB3  1 
ATOM   1895 H  HG2  . LYS   A 1 90  ? 31.714 -3.424  16.629  1.00 29.80 ?  90  LYS   A HG2  1 
ATOM   1896 H  HG3  . LYS   A 1 90  ? 31.523 -2.536  17.937  1.00 29.80 ?  90  LYS   A HG3  1 
ATOM   1897 H  HD2  . LYS   A 1 90  ? 30.818 -4.551  19.052  1.00 36.75 ?  90  LYS   A HD2  1 
ATOM   1898 H  HD3  . LYS   A 1 90  ? 31.354 -5.344  17.781  1.00 36.75 ?  90  LYS   A HD3  1 
ATOM   1899 H  HE2  . LYS   A 1 90  ? 33.056 -3.664  19.265  1.00 41.85 ?  90  LYS   A HE2  1 
ATOM   1900 H  HE3  . LYS   A 1 90  ? 32.900 -5.203  19.627  1.00 41.85 ?  90  LYS   A HE3  1 
ATOM   1901 H  HZ1  . LYS   A 1 90  ? 34.712 -4.881  18.302  1.00 45.27 ?  90  LYS   A HZ1  1 
ATOM   1902 H  HZ2  . LYS   A 1 90  ? 33.759 -5.700  17.580  1.00 45.27 ?  90  LYS   A HZ2  1 
ATOM   1903 H  HZ3  . LYS   A 1 90  ? 33.903 -4.296  17.251  1.00 45.27 ?  90  LYS   A HZ3  1 
ATOM   1904 N  N    . HIS   A 1 91  ? 29.646 -2.339  14.145  1.00 13.74 ?  91  HIS   A N    1 
ATOM   1905 C  CA   . HIS   A 1 91  ? 30.225 -2.324  12.815  1.00 13.09 ?  91  HIS   A CA   1 
ATOM   1906 C  C    . HIS   A 1 91  ? 29.144 -2.046  11.787  1.00 11.91 ?  91  HIS   A C    1 
ATOM   1907 O  O    . HIS   A 1 91  ? 27.977 -2.400  11.980  1.00 12.76 ?  91  HIS   A O    1 
ATOM   1908 C  CB   . HIS   A 1 91  ? 30.823 -3.690  12.454  1.00 15.55 ?  91  HIS   A CB   1 
ATOM   1909 C  CG   . HIS   A 1 91  ? 31.805 -4.210  13.454  1.00 19.70 ?  91  HIS   A CG   1 
ATOM   1910 N  ND1  . HIS   A 1 91  ? 33.092 -3.728  13.553  1.00 21.93 ?  91  HIS   A ND1  1 
ATOM   1911 C  CD2  . HIS   A 1 91  ? 31.694 -5.181  14.391  1.00 21.76 ?  91  HIS   A CD2  1 
ATOM   1912 C  CE1  . HIS   A 1 91  ? 33.731 -4.377  14.511  1.00 23.02 ?  91  HIS   A CE1  1 
ATOM   1913 N  NE2  . HIS   A 1 91  ? 32.905 -5.265  15.035  1.00 23.16 ?  91  HIS   A NE2  1 
ATOM   1914 H  H    . HIS   A 1 91  ? 28.967 -2.880  14.211  1.00 16.47 ?  91  HIS   A H    1 
ATOM   1915 H  HA   . HIS   A 1 91  ? 30.913 -1.649  12.757  1.00 15.69 ?  91  HIS   A HA   1 
ATOM   1916 H  HB2  . HIS   A 1 91  ? 30.104 -4.340  12.384  1.00 18.64 ?  91  HIS   A HB2  1 
ATOM   1917 H  HB3  . HIS   A 1 91  ? 31.279 -3.616  11.601  1.00 18.64 ?  91  HIS   A HB3  1 
ATOM   1918 H  HD1  . HIS   A 1 91  ? 33.428 -3.103  13.063  1.00 26.29 ?  91  HIS   A HD1  1 
ATOM   1919 H  HD2  . HIS   A 1 91  ? 30.945 -5.695  14.569  1.00 26.10 ?  91  HIS   A HD2  1 
ATOM   1920 H  HE1  . HIS   A 1 91  ? 34.616 -4.227  14.769  1.00 27.60 ?  91  HIS   A HE1  1 
ATOM   1921 N  N    . CYS   A 1 92  ? 29.552 -1.450  10.674  1.00 11.75 ?  92  CYS   A N    1 
ATOM   1922 C  CA   . CYS   A 1 92  ? 28.727 -1.374  9.480   1.00 11.38 ?  92  CYS   A CA   1 
ATOM   1923 C  C    . CYS   A 1 92  ? 29.378 -2.192  8.375   1.00 11.01 ?  92  CYS   A C    1 
ATOM   1924 O  O    . CYS   A 1 92  ? 30.538 -1.943  8.012   1.00 11.79 ?  92  CYS   A O    1 
ATOM   1925 C  CB   . CYS   A 1 92  ? 28.509 0.069   9.022   1.00 11.84 ?  92  CYS   A CB   1 
ATOM   1926 S  SG   . CYS   A 1 92  ? 27.509 0.175   7.505   1.00 11.13 ?  92  CYS   A SG   1 
ATOM   1927 H  H    . CYS   A 1 92  ? 30.326 -1.073  10.589  1.00 14.09 ?  92  CYS   A H    1 
ATOM   1928 H  HA   . CYS   A 1 92  ? 27.862 -1.757  9.673   1.00 13.64 ?  92  CYS   A HA   1 
ATOM   1929 H  HB2  . CYS   A 1 92  ? 28.043 0.562   9.719   1.00 14.19 ?  92  CYS   A HB2  1 
ATOM   1930 H  HB3  . CYS   A 1 92  ? 29.367 0.485   8.843   1.00 14.19 ?  92  CYS   A HB3  1 
ATOM   1931 H  HG   . CYS   A 1 92  ? 27.369 1.326   7.212   1.00 13.34 ?  92  CYS   A HG   1 
ATOM   1932 N  N    . LEU   A 1 93  ? 28.644 -3.183  7.873   1.00 10.84 ?  93  LEU   A N    1 
ATOM   1933 C  CA   . LEU   A 1 93  ? 29.044 -3.939  6.693   1.00 10.59 ?  93  LEU   A CA   1 
ATOM   1934 C  C    . LEU   A 1 93  ? 28.451 -3.248  5.467   1.00 10.18 ?  93  LEU   A C    1 
ATOM   1935 O  O    . LEU   A 1 93  ? 27.238 -3.308  5.235   1.00 10.40 ?  93  LEU   A O    1 
ATOM   1936 C  CB   . LEU   A 1 93  ? 28.568 -5.386  6.804   1.00 11.32 ?  93  LEU   A CB   1 
ATOM   1937 C  CG   . LEU   A 1 93  ? 28.959 -6.288  5.636   1.00 11.45 ?  93  LEU   A CG   1 
ATOM   1938 C  CD1  . LEU   A 1 93  ? 30.461 -6.549  5.633   1.00 12.52 ?  93  LEU   A CD1  1 
ATOM   1939 C  CD2  . LEU   A 1 93  ? 28.177 -7.606  5.686   1.00 12.16 ?  93  LEU   A CD2  1 
ATOM   1940 H  H    . LEU   A 1 93  ? 27.894 -3.434  8.213   1.00 13.00 ?  93  LEU   A H    1 
ATOM   1941 H  HA   . LEU   A 1 93  ? 30.008 -3.927  6.620   1.00 12.70 ?  93  LEU   A HA   1 
ATOM   1942 H  HB2  . LEU   A 1 93  ? 28.945 -5.767  7.615   1.00 13.56 ?  93  LEU   A HB2  1 
ATOM   1943 H  HB3  . LEU   A 1 93  ? 27.602 -5.388  6.865   1.00 13.56 ?  93  LEU   A HB3  1 
ATOM   1944 H  HG   . LEU   A 1 93  ? 28.742 -5.848  4.808   1.00 13.73 ?  93  LEU   A HG   1 
ATOM   1945 H  HD11 . LEU   A 1 93  ? 30.676 -7.165  4.914   1.00 15.01 ?  93  LEU   A HD11 1 
ATOM   1946 H  HD12 . LEU   A 1 93  ? 30.930 -5.713  5.505   1.00 15.01 ?  93  LEU   A HD12 1 
ATOM   1947 H  HD13 . LEU   A 1 93  ? 30.718 -6.945  6.486   1.00 15.01 ?  93  LEU   A HD13 1 
ATOM   1948 H  HD21 . LEU   A 1 93  ? 28.447 -8.164  4.938   1.00 14.58 ?  93  LEU   A HD21 1 
ATOM   1949 H  HD22 . LEU   A 1 93  ? 28.369 -8.061  6.522   1.00 14.58 ?  93  LEU   A HD22 1 
ATOM   1950 H  HD23 . LEU   A 1 93  ? 27.229 -7.411  5.626   1.00 14.58 ?  93  LEU   A HD23 1 
ATOM   1951 N  N    . HIS   A 1 94  ? 29.303 -2.561  4.706   1.00 9.97  ?  94  HIS   A N    1 
ATOM   1952 C  CA   . HIS   A 1 94  ? 28.887 -1.889  3.478   1.00 10.13 ?  94  HIS   A CA   1 
ATOM   1953 C  C    . HIS   A 1 94  ? 28.903 -2.925  2.369   1.00 10.26 ?  94  HIS   A C    1 
ATOM   1954 O  O    . HIS   A 1 94  ? 29.969 -3.438  2.024   1.00 11.63 ?  94  HIS   A O    1 
ATOM   1955 C  CB   . HIS   A 1 94  ? 29.847 -0.745  3.152   1.00 10.15 ?  94  HIS   A CB   1 
ATOM   1956 C  CG   . HIS   A 1 94  ? 29.832 0.347   4.167   1.00 9.89  ?  94  HIS   A CG   1 
ATOM   1957 N  ND1  . HIS   A 1 94  ? 28.960 1.414   4.105   1.00 10.29 ?  94  HIS   A ND1  1 
ATOM   1958 C  CD2  . HIS   A 1 94  ? 30.568 0.523   5.287   1.00 11.04 ?  94  HIS   A CD2  1 
ATOM   1959 C  CE1  . HIS   A 1 94  ? 29.167 2.199   5.147   1.00 10.63 ?  94  HIS   A CE1  1 
ATOM   1960 N  NE2  . HIS   A 1 94  ? 30.139 1.682   5.878   1.00 10.99 ?  94  HIS   A NE2  1 
ATOM   1961 H  H    . HIS   A 1 94  ? 30.138 -2.464  4.884   1.00 11.95 ?  94  HIS   A H    1 
ATOM   1962 H  HA   . HIS   A 1 94  ? 27.982 -1.536  3.577   1.00 12.14 ?  94  HIS   A HA   1 
ATOM   1963 H  HB2  . HIS   A 1 94  ? 30.742 -1.095  3.106   1.00 12.17 ?  94  HIS   A HB2  1 
ATOM   1964 H  HB3  . HIS   A 1 94  ? 29.590 -0.358  2.300   1.00 12.17 ?  94  HIS   A HB3  1 
ATOM   1965 H  HD2  . HIS   A 1 94  ? 31.239 -0.029  5.600   1.00 13.23 ?  94  HIS   A HD2  1 
ATOM   1966 H  HE1  . HIS   A 1 94  ? 28.699 2.989   5.328   1.00 12.74 ?  94  HIS   A HE1  1 
ATOM   1967 H  HE2  . HIS   A 1 94  ? 30.446 2.031   6.600   1.00 13.18 ?  94  HIS   A HE2  1 
ATOM   1968 N  N    . VAL   A 1 95  ? 27.731 -3.247  1.823   1.00 9.50  ?  95  VAL   A N    1 
ATOM   1969 C  CA   . VAL   A 1 95  ? 27.584 -4.281  0.804   1.00 9.82  ?  95  VAL   A CA   1 
ATOM   1970 C  C    . VAL   A 1 95  ? 27.043 -3.646  -0.465  1.00 9.54  ?  95  VAL   A C    1 
ATOM   1971 O  O    . VAL   A 1 95  ? 26.039 -2.928  -0.415  1.00 10.40 ?  95  VAL   A O    1 
ATOM   1972 C  CB   . VAL   A 1 95  ? 26.654 -5.422  1.259   1.00 10.36 ?  95  VAL   A CB   1 
ATOM   1973 C  CG1  . VAL   A 1 95  ? 26.554 -6.465  0.164   1.00 11.41 ?  95  VAL   A CG1  1 
ATOM   1974 C  CG2  . VAL   A 1 95  ? 27.156 -6.041  2.548   1.00 10.82 ?  95  VAL   A CG2  1 
ATOM   1975 H  H    . VAL   A 1 95  ? 26.982 -2.876  2.036   1.00 11.38 ?  95  VAL   A H    1 
ATOM   1976 H  HA   . VAL   A 1 95  ? 28.449 -4.663  0.605   1.00 11.76 ?  95  VAL   A HA   1 
ATOM   1977 H  HB   . VAL   A 1 95  ? 25.765 -5.074  1.420   1.00 12.42 ?  95  VAL   A HB   1 
ATOM   1978 H  HG11 . VAL   A 1 95  ? 26.164 -7.279  0.530   1.00 13.67 ?  95  VAL   A HG11 1 
ATOM   1979 H  HG12 . VAL   A 1 95  ? 25.990 -6.131  -0.552  1.00 13.67 ?  95  VAL   A HG12 1 
ATOM   1980 H  HG13 . VAL   A 1 95  ? 27.442 -6.658  -0.178  1.00 13.67 ?  95  VAL   A HG13 1 
ATOM   1981 H  HG21 . VAL   A 1 95  ? 26.593 -6.801  2.776   1.00 12.97 ?  95  VAL   A HG21 1 
ATOM   1982 H  HG22 . VAL   A 1 95  ? 28.071 -6.337  2.422   1.00 12.97 ?  95  VAL   A HG22 1 
ATOM   1983 H  HG23 . VAL   A 1 95  ? 27.115 -5.378  3.252   1.00 12.97 ?  95  VAL   A HG23 1 
ATOM   1984 N  N    . VAL   A 1 96  ? 27.678 -3.933  -1.598  1.00 9.71  ?  96  VAL   A N    1 
ATOM   1985 C  CA   . VAL   A 1 96  ? 27.273 -3.384  -2.887  1.00 10.43 ?  96  VAL   A CA   1 
ATOM   1986 C  C    . VAL   A 1 96  ? 26.465 -4.437  -3.641  1.00 10.79 ?  96  VAL   A C    1 
ATOM   1987 O  O    . VAL   A 1 96  ? 27.024 -5.387  -4.202  1.00 11.77 ?  96  VAL   A O    1 
ATOM   1988 C  CB   . VAL   A 1 96  ? 28.473 -2.912  -3.711  1.00 10.72 ?  96  VAL   A CB   1 
ATOM   1989 C  CG1  . VAL   A 1 96  ? 27.975 -2.275  -4.985  1.00 11.10 ?  96  VAL   A CG1  1 
ATOM   1990 C  CG2  . VAL   A 1 96  ? 29.337 -1.942  -2.917  1.00 11.39 ?  96  VAL   A CG2  1 
ATOM   1991 H  H    . VAL   A 1 96  ? 28.374 -4.444  -1.641  1.00 11.63 ?  96  VAL   A H    1 
ATOM   1992 H  HA   . VAL   A 1 96  ? 26.702 -2.616  -2.731  1.00 12.51 ?  96  VAL   A HA   1 
ATOM   1993 H  HB   . VAL   A 1 96  ? 29.019 -3.673  -3.945  1.00 12.85 ?  96  VAL   A HB   1 
ATOM   1994 H  HG11 . VAL   A 1 96  ? 28.715 -1.806  -5.405  1.00 13.31 ?  96  VAL   A HG11 1 
ATOM   1995 H  HG12 . VAL   A 1 96  ? 27.642 -2.965  -5.572  1.00 13.31 ?  96  VAL   A HG12 1 
ATOM   1996 H  HG13 . VAL   A 1 96  ? 27.270 -1.645  -4.767  1.00 13.31 ?  96  VAL   A HG13 1 
ATOM   1997 H  HG21 . VAL   A 1 96  ? 30.045 -1.604  -3.486  1.00 13.65 ?  96  VAL   A HG21 1 
ATOM   1998 H  HG22 . VAL   A 1 96  ? 28.787 -1.204  -2.602  1.00 13.65 ?  96  VAL   A HG22 1 
ATOM   1999 H  HG23 . VAL   A 1 96  ? 29.723 -2.407  -2.154  1.00 13.65 ?  96  VAL   A HG23 1 
ATOM   2000 N  N    . GLY   A 1 97  ? 25.146 -4.273  -3.675  1.00 10.97 ?  97  GLY   A N    1 
ATOM   2001 C  CA   . GLY   A 1 97  ? 24.335 -5.039  -4.583  1.00 11.24 ?  97  GLY   A CA   1 
ATOM   2002 C  C    . GLY   A 1 97  ? 24.335 -4.388  -5.950  1.00 11.57 ?  97  GLY   A C    1 
ATOM   2003 O  O    . GLY   A 1 97  ? 24.617 -3.191  -6.088  1.00 12.34 ?  97  GLY   A O    1 
ATOM   2004 H  H    . GLY   A 1 97  ? 24.710 -3.718  -3.177  1.00 13.15 ?  97  GLY   A H    1 
ATOM   2005 H  HA2  . GLY   A 1 97  ? 24.696 -5.938  -4.651  1.00 13.47 ?  97  GLY   A HA2  1 
ATOM   2006 H  HA3  . GLY   A 1 97  ? 23.428 -5.089  -4.246  1.00 13.47 ?  97  GLY   A HA3  1 
ATOM   2007 N  N    . PRO   A 1 98  ? 24.018 -5.152  -6.990  1.00 11.54 ?  98  PRO   A N    1 
ATOM   2008 C  CA   . PRO   A 1 98  ? 23.920 -4.556  -8.324  1.00 13.09 ?  98  PRO   A CA   1 
ATOM   2009 C  C    . PRO   A 1 98  ? 22.806 -3.523  -8.406  1.00 13.42 ?  98  PRO   A C    1 
ATOM   2010 O  O    . PRO   A 1 98  ? 21.720 -3.689  -7.842  1.00 13.33 ?  98  PRO   A O    1 
ATOM   2011 C  CB   . PRO   A 1 98  ? 23.635 -5.761  -9.228  1.00 13.33 ?  98  PRO   A CB   1 
ATOM   2012 C  CG   . PRO   A 1 98  ? 22.990 -6.762  -8.326  1.00 13.31 ?  98  PRO   A CG   1 
ATOM   2013 C  CD   . PRO   A 1 98  ? 23.707 -6.593  -7.004  1.00 11.90 ?  98  PRO   A CD   1 
ATOM   2014 H  HA   . PRO   A 1 98  ? 24.765 -4.153  -8.572  1.00 15.70 ?  98  PRO   A HA   1 
ATOM   2015 H  HB2  . PRO   A 1 98  ? 23.029 -5.496  -9.937  1.00 15.98 ?  98  PRO   A HB2  1 
ATOM   2016 H  HB3  . PRO   A 1 98  ? 24.465 -6.104  -9.589  1.00 15.98 ?  98  PRO   A HB3  1 
ATOM   2017 H  HG2  . PRO   A 1 98  ? 22.047 -6.563  -8.236  1.00 15.95 ?  98  PRO   A HG2  1 
ATOM   2018 H  HG3  . PRO   A 1 98  ? 23.125 -7.654  -8.682  1.00 15.95 ?  98  PRO   A HG3  1 
ATOM   2019 H  HD2  . PRO   A 1 98  ? 23.117 -6.828  -6.267  1.00 14.26 ?  98  PRO   A HD2  1 
ATOM   2020 H  HD3  . PRO   A 1 98  ? 24.523 -7.121  -6.986  1.00 14.26 ?  98  PRO   A HD3  1 
ATOM   2021 N  N    A ASN   A 1 99  ? 23.078 -2.414  -9.097  0.70 14.52 ?  99  ASN   A N    1 
ATOM   2022 N  N    B ASN   A 1 99  ? 23.116 -2.461  -9.135  0.30 14.07 ?  99  ASN   A N    1 
ATOM   2023 C  CA   A ASN   A 1 99  ? 22.097 -1.342  -9.285  0.70 15.28 ?  99  ASN   A CA   1 
ATOM   2024 C  CA   B ASN   A 1 99  ? 22.164 -1.441  -9.534  0.30 14.55 ?  99  ASN   A CA   1 
ATOM   2025 C  C    A ASN   A 1 99  ? 21.518 -1.463  -10.690 0.70 16.68 ?  99  ASN   A C    1 
ATOM   2026 C  C    B ASN   A 1 99  ? 21.630 -1.837  -10.903 0.30 14.96 ?  99  ASN   A C    1 
ATOM   2027 O  O    A ASN   A 1 99  ? 22.179 -1.117  -11.677 0.70 17.64 ?  99  ASN   A O    1 
ATOM   2028 O  O    B ASN   A 1 99  ? 22.364 -1.825  -11.897 0.30 14.53 ?  99  ASN   A O    1 
ATOM   2029 C  CB   A ASN   A 1 99  ? 22.721 0.039   -9.069  0.70 15.58 ?  99  ASN   A CB   1 
ATOM   2030 C  CB   B ASN   A 1 99  ? 22.890 -0.105  -9.613  0.30 15.21 ?  99  ASN   A CB   1 
ATOM   2031 C  CG   A ASN   A 1 99  ? 21.680 1.174   -9.048  0.70 15.68 ?  99  ASN   A CG   1 
ATOM   2032 C  CG   B ASN   A 1 99  ? 21.967 1.036   -9.929  0.30 15.64 ?  99  ASN   A CG   1 
ATOM   2033 O  OD1  A ASN   A 1 99  ? 20.667 1.121   -9.745  0.70 15.96 ?  99  ASN   A OD1  1 
ATOM   2034 O  OD1  B ASN   A 1 99  ? 20.951 0.862   -10.598 0.30 15.72 ?  99  ASN   A OD1  1 
ATOM   2035 N  ND2  A ASN   A 1 99  ? 21.946 2.208   -8.248  0.70 16.03 ?  99  ASN   A ND2  1 
ATOM   2036 N  ND2  B ASN   A 1 99  ? 22.320 2.225   -9.452  0.30 16.48 ?  99  ASN   A ND2  1 
ATOM   2037 H  H    A ASN   A 1 99  ? 23.841 -2.253  -9.461  0.70 17.41 ?  99  ASN   A H    1 
ATOM   2038 H  H    B ASN   A 1 99  ? 23.911 -2.305  -9.420  0.30 16.87 ?  99  ASN   A H    1 
ATOM   2039 H  HA   A ASN   A 1 99  ? 21.375 -1.453  -8.646  0.70 18.32 ?  99  ASN   A HA   1 
ATOM   2040 H  HA   B ASN   A 1 99  ? 21.431 -1.386  -8.895  0.30 17.44 ?  99  ASN   A HA   1 
ATOM   2041 H  HB2  A ASN   A 1 99  ? 23.193 0.047   -8.226  0.70 18.68 ?  99  ASN   A HB2  1 
ATOM   2042 H  HB2  B ASN   A 1 99  ? 23.313 0.075   -8.762  0.30 18.24 ?  99  ASN   A HB2  1 
ATOM   2043 H  HB3  A ASN   A 1 99  ? 23.340 0.219   -9.798  0.70 18.68 ?  99  ASN   A HB3  1 
ATOM   2044 H  HB3  B ASN   A 1 99  ? 23.559 -0.157  -10.315 0.30 18.24 ?  99  ASN   A HB3  1 
ATOM   2045 H  HD21 A ASN   A 1 99  ? 21.398 2.869   -8.194  0.70 19.22 ?  99  ASN   A HD21 1 
ATOM   2046 H  HD21 B ASN   A 1 99  ? 21.834 2.917   -9.608  0.30 19.76 ?  99  ASN   A HD21 1 
ATOM   2047 H  HD22 A ASN   A 1 99  ? 22.665 2.209   -7.772  0.70 19.22 ?  99  ASN   A HD22 1 
ATOM   2048 H  HD22 B ASN   A 1 99  ? 23.042 2.307   -8.990  0.30 19.76 ?  99  ASN   A HD22 1 
ATOM   2049 N  N    A VAL   A 1 100 ? 20.273 -1.944  -10.769 0.70 17.83 ?  100 VAL   A N    1 
ATOM   2050 N  N    B VAL   A 1 100 ? 20.348 -2.189  -10.951 0.30 16.19 ?  100 VAL   A N    1 
ATOM   2051 C  CA   A VAL   A 1 100 ? 19.623 -2.159  -12.059 0.70 19.15 ?  100 VAL   A CA   1 
ATOM   2052 C  CA   B VAL   A 1 100 ? 19.748 -2.655  -12.195 0.30 17.71 ?  100 VAL   A CA   1 
ATOM   2053 C  C    A VAL   A 1 100 ? 19.508 -0.854  -12.832 0.70 19.47 ?  100 VAL   A C    1 
ATOM   2054 C  C    B VAL   A 1 100 ? 19.651 -1.521  -13.197 0.30 17.67 ?  100 VAL   A C    1 
ATOM   2055 O  O    A VAL   A 1 100 ? 19.594 -0.843  -14.066 0.70 20.29 ?  100 VAL   A O    1 
ATOM   2056 O  O    B VAL   A 1 100 ? 19.686 -1.752  -14.413 0.30 17.53 ?  100 VAL   A O    1 
ATOM   2057 C  CB   A VAL   A 1 100 ? 18.260 -2.859  -11.862 0.70 20.40 ?  100 VAL   A CB   1 
ATOM   2058 C  CB   B VAL   A 1 100 ? 18.366 -3.259  -11.910 0.30 19.34 ?  100 VAL   A CB   1 
ATOM   2059 C  CG1  A VAL   A 1 100 ? 17.521 -3.007  -13.186 0.70 20.74 ?  100 VAL   A CG1  1 
ATOM   2060 C  CG1  B VAL   A 1 100 ? 18.040 -4.321  -12.937 0.30 19.89 ?  100 VAL   A CG1  1 
ATOM   2061 C  CG2  A VAL   A 1 100 ? 18.465 -4.227  -11.221 0.70 20.58 ?  100 VAL   A CG2  1 
ATOM   2062 C  CG2  B VAL   A 1 100 ? 18.329 -3.823  -10.506 0.30 19.99 ?  100 VAL   A CG2  1 
ATOM   2063 H  H    A VAL   A 1 100 ? 19.780 -2.149  -10.089 0.70 21.38 ?  100 VAL   A H    1 
ATOM   2064 H  H    B VAL   A 1 100 ? 19.819 -2.152  -10.277 0.30 19.41 ?  100 VAL   A H    1 
ATOM   2065 H  HA   A VAL   A 1 100 ? 20.172 -2.756  -12.585 0.70 22.96 ?  100 VAL   A HA   1 
ATOM   2066 H  HA   B VAL   A 1 100 ? 20.306 -3.347  -12.587 0.30 21.24 ?  100 VAL   A HA   1 
ATOM   2067 H  HB   A VAL   A 1 100 ? 17.706 -2.330  -11.268 0.70 24.47 ?  100 VAL   A HB   1 
ATOM   2068 H  HB   B VAL   A 1 100 ? 17.695 -2.557  -11.980 0.30 23.19 ?  100 VAL   A HB   1 
ATOM   2069 H  HG11 A VAL   A 1 100 ? 16.771 -3.614  -13.065 0.70 24.87 ?  100 VAL   A HG11 1 
ATOM   2070 H  HG11 B VAL   A 1 100 ? 17.154 -4.667  -12.757 0.30 23.85 ?  100 VAL   A HG11 1 
ATOM   2071 H  HG12 A VAL   A 1 100 ? 17.196 -2.138  -13.468 0.70 24.87 ?  100 VAL   A HG12 1 
ATOM   2072 H  HG12 B VAL   A 1 100 ? 18.071 -3.926  -13.822 0.30 23.85 ?  100 VAL   A HG12 1 
ATOM   2073 H  HG13 A VAL   A 1 100 ? 18.129 -3.367  -13.850 0.70 24.87 ?  100 VAL   A HG13 1 
ATOM   2074 H  HG13 B VAL   A 1 100 ? 18.697 -5.031  -12.868 0.30 23.85 ?  100 VAL   A HG13 1 
ATOM   2075 H  HG21 A VAL   A 1 100 ? 17.608 -4.678  -11.151 0.70 24.68 ?  100 VAL   A HG21 1 
ATOM   2076 H  HG21 B VAL   A 1 100 ? 17.615 -4.459  -10.453 0.30 23.98 ?  100 VAL   A HG21 1 
ATOM   2077 H  HG22 A VAL   A 1 100 ? 19.067 -4.748  -11.776 0.70 24.68 ?  100 VAL   A HG22 1 
ATOM   2078 H  HG22 B VAL   A 1 100 ? 19.179 -4.255  -10.317 0.30 23.98 ?  100 VAL   A HG22 1 
ATOM   2079 H  HG23 A VAL   A 1 100 ? 18.849 -4.107  -10.338 0.70 24.68 ?  100 VAL   A HG23 1 
ATOM   2080 H  HG23 B VAL   A 1 100 ? 18.178 -3.096  -9.878  0.30 23.98 ?  100 VAL   A HG23 1 
ATOM   2081 N  N    A ASN   A 1 101 ? 19.323 0.265   -12.136 0.70 20.27 ?  101 ASN   A N    1 
ATOM   2082 N  N    B ASN   A 1 101 ? 19.508 -0.285  -12.712 0.30 18.06 ?  101 ASN   A N    1 
ATOM   2083 C  CA   A ASN   A 1 101 ? 19.258 1.547   -12.824 0.70 21.48 ?  101 ASN   A CA   1 
ATOM   2084 C  CA   B ASN   A 1 101 ? 19.417 0.867   -13.600 0.30 18.43 ?  101 ASN   A CA   1 
ATOM   2085 C  C    A ASN   A 1 101 ? 20.611 1.991   -13.378 0.70 23.76 ?  101 ASN   A C    1 
ATOM   2086 C  C    B ASN   A 1 101 ? 20.728 1.137   -14.322 0.30 19.37 ?  101 ASN   A C    1 
ATOM   2087 O  O    A ASN   A 1 101 ? 20.675 3.045   -14.024 0.70 25.50 ?  101 ASN   A O    1 
ATOM   2088 O  O    B ASN   A 1 101 ? 20.717 1.775   -15.379 0.30 19.33 ?  101 ASN   A O    1 
ATOM   2089 C  CB   A ASN   A 1 101 ? 18.641 2.596   -11.898 0.70 20.64 ?  101 ASN   A CB   1 
ATOM   2090 C  CB   B ASN   A 1 101 ? 18.990 2.104   -12.806 0.30 18.13 ?  101 ASN   A CB   1 
ATOM   2091 C  CG   A ASN   A 1 101 ? 17.263 2.180   -11.393 0.70 20.21 ?  101 ASN   A CG   1 
ATOM   2092 C  CG   B ASN   A 1 101 ? 17.760 1.851   -11.954 0.30 18.70 ?  101 ASN   A CG   1 
ATOM   2093 O  OD1  A ASN   A 1 101 ? 16.431 1.687   -12.157 0.70 20.34 ?  101 ASN   A OD1  1 
ATOM   2094 O  OD1  B ASN   A 1 101 ? 16.817 1.184   -12.382 0.30 19.43 ?  101 ASN   A OD1  1 
ATOM   2095 N  ND2  A ASN   A 1 101 ? 17.026 2.357   -10.101 0.70 20.11 ?  101 ASN   A ND2  1 
ATOM   2096 N  ND2  B ASN   A 1 101 ? 17.771 2.373   -10.736 0.30 18.75 ?  101 ASN   A ND2  1 
ATOM   2097 H  H    A ASN   A 1 101 ? 19.228 0.307   -11.286 0.70 24.31 ?  101 ASN   A H    1 
ATOM   2098 H  H    B ASN   A 1 101 ? 19.465 -0.085  -11.874 0.30 21.66 ?  101 ASN   A H    1 
ATOM   2099 H  HA   A ASN   A 1 101 ? 18.664 1.453   -13.583 0.70 25.76 ?  101 ASN   A HA   1 
ATOM   2100 H  HA   B ASN   A 1 101 ? 18.741 0.700   -14.270 0.30 22.10 ?  101 ASN   A HA   1 
ATOM   2101 H  HB2  A ASN   A 1 101 ? 19.220 2.726   -11.133 0.70 24.75 ?  101 ASN   A HB2  1 
ATOM   2102 H  HB2  B ASN   A 1 101 ? 19.712 2.374   -12.216 0.30 21.74 ?  101 ASN   A HB2  1 
ATOM   2103 H  HB3  A ASN   A 1 101 ? 18.547 3.433   -12.388 0.70 24.75 ?  101 ASN   A HB3  1 
ATOM   2104 H  HB3  B ASN   A 1 101 ? 18.782 2.827   -13.423 0.30 21.74 ?  101 ASN   A HB3  1 
ATOM   2105 H  HD21 A ASN   A 1 101 ? 16.264 2.136   -9.772  0.70 24.12 ?  101 ASN   A HD21 1 
ATOM   2106 H  HD21 B ASN   A 1 101 ? 17.097 2.257   -10.215 0.30 22.48 ?  101 ASN   A HD21 1 
ATOM   2107 H  HD22 A ASN   A 1 101 ? 17.631 2.700   -9.597  0.70 24.12 ?  101 ASN   A HD22 1 
ATOM   2108 H  HD22 B ASN   A 1 101 ? 18.446 2.836   -10.470 0.30 22.48 ?  101 ASN   A HD22 1 
ATOM   2109 N  N    A LYS   A 1 102 ? 21.673 1.205   -13.162 0.70 25.33 ?  102 LYS   A N    1 
ATOM   2110 N  N    B LYS   A 1 102 ? 21.849 0.676   -13.773 0.30 20.69 ?  102 LYS   A N    1 
ATOM   2111 C  CA   A LYS   A 1 102 ? 22.966 1.403   -13.807 0.70 26.57 ?  102 LYS   A CA   1 
ATOM   2112 C  CA   B LYS   A 1 102 ? 23.145 0.771   -14.427 0.30 21.68 ?  102 LYS   A CA   1 
ATOM   2113 C  C    A LYS   A 1 102 ? 23.297 0.310   -14.814 0.70 27.37 ?  102 LYS   A C    1 
ATOM   2114 C  C    B LYS   A 1 102 ? 23.456 -0.452  -15.280 0.30 21.26 ?  102 LYS   A C    1 
ATOM   2115 O  O    A LYS   A 1 102 ? 24.378 0.348   -15.410 0.70 27.99 ?  102 LYS   A O    1 
ATOM   2116 O  O    B LYS   A 1 102 ? 24.588 -0.591  -15.755 0.30 20.88 ?  102 LYS   A O    1 
ATOM   2117 C  CB   A LYS   A 1 102 ? 24.088 1.459   -12.762 0.70 27.72 ?  102 LYS   A CB   1 
ATOM   2118 C  CB   B LYS   A 1 102 ? 24.255 0.965   -13.388 0.30 23.37 ?  102 LYS   A CB   1 
ATOM   2119 C  CG   A LYS   A 1 102 ? 23.972 2.587   -11.760 0.70 28.55 ?  102 LYS   A CG   1 
ATOM   2120 C  CG   B LYS   A 1 102 ? 24.155 2.255   -12.587 0.30 24.83 ?  102 LYS   A CG   1 
ATOM   2121 C  CD   A LYS   A 1 102 ? 25.129 2.546   -10.771 0.70 29.62 ?  102 LYS   A CD   1 
ATOM   2122 C  CD   B LYS   A 1 102 ? 25.372 2.438   -11.686 0.30 26.38 ?  102 LYS   A CD   1 
ATOM   2123 C  CE   A LYS   A 1 102 ? 25.049 3.680   -9.765  0.70 30.69 ?  102 LYS   A CE   1 
ATOM   2124 C  CE   B LYS   A 1 102 ? 25.349 3.781   -10.970 0.30 27.51 ?  102 LYS   A CE   1 
ATOM   2125 N  NZ   A LYS   A 1 102 ? 26.137 3.593   -8.749  0.70 31.11 ?  102 LYS   A NZ   1 
ATOM   2126 N  NZ   B LYS   A 1 102 ? 26.619 4.054   -10.236 0.30 28.13 ?  102 LYS   A NZ   1 
ATOM   2127 H  H    A LYS   A 1 102 ? 21.666 0.525   -12.635 0.70 30.39 ?  102 LYS   A H    1 
ATOM   2128 H  H    B LYS   A 1 102 ? 21.881 0.298   -13.002 0.30 24.81 ?  102 LYS   A H    1 
ATOM   2129 H  HA   A LYS   A 1 102 ? 22.962 2.242   -14.284 0.70 31.87 ?  102 LYS   A HA   1 
ATOM   2130 H  HA   B LYS   A 1 102 ? 23.150 1.550   -15.002 0.30 26.00 ?  102 LYS   A HA   1 
ATOM   2131 H  HB2  A LYS   A 1 102 ? 24.092 0.625   -12.267 0.70 33.25 ?  102 LYS   A HB2  1 
ATOM   2132 H  HB2  B LYS   A 1 102 ? 24.222 0.231   -12.757 0.30 28.03 ?  102 LYS   A HB2  1 
ATOM   2133 H  HB3  A LYS   A 1 102 ? 24.936 1.564   -13.224 0.70 33.25 ?  102 LYS   A HB3  1 
ATOM   2134 H  HB3  B LYS   A 1 102 ? 25.113 0.968   -13.844 0.30 28.03 ?  102 LYS   A HB3  1 
ATOM   2135 H  HG2  A LYS   A 1 102 ? 23.996 3.436   -12.228 0.70 34.24 ?  102 LYS   A HG2  1 
ATOM   2136 H  HG2  B LYS   A 1 102 ? 24.110 3.010   -13.194 0.30 29.78 ?  102 LYS   A HG2  1 
ATOM   2137 H  HG3  A LYS   A 1 102 ? 23.141 2.494   -11.268 0.70 34.24 ?  102 LYS   A HG3  1 
ATOM   2138 H  HG3  B LYS   A 1 102 ? 23.363 2.226   -12.027 0.30 29.78 ?  102 LYS   A HG3  1 
ATOM   2139 H  HD2  A LYS   A 1 102 ? 25.104 1.706   -10.285 0.70 35.53 ?  102 LYS   A HD2  1 
ATOM   2140 H  HD2  B LYS   A 1 102 ? 25.381 1.736   -11.016 0.30 31.63 ?  102 LYS   A HD2  1 
ATOM   2141 H  HD3  A LYS   A 1 102 ? 25.966 2.627   -11.256 0.70 35.53 ?  102 LYS   A HD3  1 
ATOM   2142 H  HD3  B LYS   A 1 102 ? 26.177 2.395   -12.225 0.30 31.63 ?  102 LYS   A HD3  1 
ATOM   2143 H  HE2  A LYS   A 1 102 ? 25.135 4.526   -10.233 0.70 36.81 ?  102 LYS   A HE2  1 
ATOM   2144 H  HE2  B LYS   A 1 102 ? 25.220 4.487   -11.622 0.30 33.00 ?  102 LYS   A HE2  1 
ATOM   2145 H  HE3  A LYS   A 1 102 ? 24.196 3.637   -9.305  0.70 36.81 ?  102 LYS   A HE3  1 
ATOM   2146 H  HE3  B LYS   A 1 102 ? 24.623 3.785   -10.326 0.30 33.00 ?  102 LYS   A HE3  1 
ATOM   2147 H  HZ1  A LYS   A 1 102 ? 26.069 4.266   -8.173  0.70 37.32 ?  102 LYS   A HZ1  1 
ATOM   2148 H  HZ1  B LYS   A 1 102 ? 26.573 4.845   -9.829  0.30 33.74 ?  102 LYS   A HZ1  1 
ATOM   2149 H  HZ2  A LYS   A 1 102 ? 26.076 2.823   -8.305  0.70 37.32 ?  102 LYS   A HZ2  1 
ATOM   2150 H  HZ2  B LYS   A 1 102 ? 26.760 3.423   -9.624  0.30 33.74 ?  102 LYS   A HZ2  1 
ATOM   2151 H  HZ3  A LYS   A 1 102 ? 26.931 3.633   -9.150  0.70 37.32 ?  102 LYS   A HZ3  1 
ATOM   2152 H  HZ3  B LYS   A 1 102 ? 27.304 4.062   -10.804 0.30 33.74 ?  102 LYS   A HZ3  1 
ATOM   2153 N  N    A GLY   A 1 103 ? 22.413 -0.668  -15.009 0.70 28.20 ?  103 GLY   A N    1 
ATOM   2154 N  N    B GLY   A 1 103 ? 22.489 -1.346  -15.475 0.30 21.35 ?  103 GLY   A N    1 
ATOM   2155 C  CA   A GLY   A 1 103 ? 22.671 -1.751  -15.938 0.70 28.39 ?  103 GLY   A CA   1 
ATOM   2156 C  CA   B GLY   A 1 103 ? 22.735 -2.533  -16.266 0.30 21.48 ?  103 GLY   A CA   1 
ATOM   2157 C  C    A GLY   A 1 103 ? 23.532 -2.869  -15.397 0.70 28.39 ?  103 GLY   A C    1 
ATOM   2158 C  C    B GLY   A 1 103 ? 23.557 -3.595  -15.576 0.30 20.95 ?  103 GLY   A C    1 
ATOM   2159 O  O    A GLY   A 1 103 ? 24.138 -3.601  -16.185 0.70 29.28 ?  103 GLY   A O    1 
ATOM   2160 O  O    B GLY   A 1 103 ? 23.972 -4.558  -16.228 0.30 20.78 ?  103 GLY   A O    1 
ATOM   2161 H  H    A GLY   A 1 103 ? 21.657 -0.729  -14.611 0.70 33.83 ?  103 GLY   A H    1 
ATOM   2162 H  H    B GLY   A 1 103 ? 21.690 -1.285  -15.154 0.30 25.61 ?  103 GLY   A H    1 
ATOM   2163 H  HA2  A GLY   A 1 103 ? 21.822 -2.125  -16.237 0.70 34.05 ?  103 GLY   A HA2  1 
ATOM   2164 H  HA2  B GLY   A 1 103 ? 21.891 -2.933  -16.512 0.30 25.77 ?  103 GLY   A HA2  1 
ATOM   2165 H  HA3  A GLY   A 1 103 ? 23.128 -1.400  -16.717 0.70 34.05 ?  103 GLY   A HA3  1 
ATOM   2166 H  HA3  B GLY   A 1 103 ? 23.194 -2.269  -17.082 0.30 25.77 ?  103 GLY   A HA3  1 
ATOM   2167 N  N    A GLU   A 1 104 ? 23.610 -3.027  -14.079 0.70 26.70 ?  104 GLU   A N    1 
ATOM   2168 N  N    B GLU   A 1 104 ? 23.795 -3.459  -14.275 0.30 20.43 ?  104 GLU   A N    1 
ATOM   2169 C  CA   A GLU   A 1 104 ? 24.479 -4.029  -13.476 0.70 24.94 ?  104 GLU   A CA   1 
ATOM   2170 C  CA   B GLU   A 1 104 ? 24.676 -4.388  -13.582 0.30 19.89 ?  104 GLU   A CA   1 
ATOM   2171 C  C    A GLU   A 1 104 ? 23.786 -5.388  -13.382 0.70 25.20 ?  104 GLU   A C    1 
ATOM   2172 C  C    B GLU   A 1 104 ? 23.989 -5.738  -13.391 0.30 20.43 ?  104 GLU   A C    1 
ATOM   2173 O  O    A GLU   A 1 104 ? 22.558 -5.483  -13.286 0.70 25.42 ?  104 GLU   A O    1 
ATOM   2174 O  O    B GLU   A 1 104 ? 22.801 -5.815  -13.062 0.30 20.19 ?  104 GLU   A O    1 
ATOM   2175 C  CB   A GLU   A 1 104 ? 24.971 -3.543  -12.108 0.70 23.02 ?  104 GLU   A CB   1 
ATOM   2176 C  CB   B GLU   A 1 104 ? 25.120 -3.787  -12.247 0.30 19.36 ?  104 GLU   A CB   1 
ATOM   2177 C  CG   A GLU   A 1 104 ? 25.942 -2.361  -12.252 0.70 21.92 ?  104 GLU   A CG   1 
ATOM   2178 C  CG   B GLU   A 1 104 ? 25.727 -2.391  -12.404 0.30 19.53 ?  104 GLU   A CG   1 
ATOM   2179 C  CD   A GLU   A 1 104 ? 26.222 -1.573  -10.976 0.70 20.96 ?  104 GLU   A CD   1 
ATOM   2180 C  CD   B GLU   A 1 104 ? 26.263 -1.802  -11.110 0.30 19.46 ?  104 GLU   A CD   1 
ATOM   2181 O  OE1  A GLU   A 1 104 ? 25.639 -1.865  -9.913  0.70 19.48 ?  104 GLU   A OE1  1 
ATOM   2182 O  OE1  B GLU   A 1 104 ? 25.843 -2.238  -10.019 0.30 19.42 ?  104 GLU   A OE1  1 
ATOM   2183 O  OE2  A GLU   A 1 104 ? 27.044 -0.630  -11.058 0.70 22.22 -1 104 GLU   A OE2  1 
ATOM   2184 O  OE2  B GLU   A 1 104 ? 27.109 -0.887  -11.193 0.30 19.80 -1 104 GLU   A OE2  1 
ATOM   2185 H  H    A GLU   A 1 104 ? 23.175 -2.551  -13.509 0.70 32.03 ?  104 GLU   A H    1 
ATOM   2186 H  H    B GLU   A 1 104 ? 23.455 -2.839  -13.778 0.30 24.50 ?  104 GLU   A H    1 
ATOM   2187 H  HA   A GLU   A 1 104 ? 25.254 -4.137  -14.046 0.70 29.92 ?  104 GLU   A HA   1 
ATOM   2188 H  HA   B GLU   A 1 104 ? 25.470 -4.527  -14.123 0.30 23.85 ?  104 GLU   A HA   1 
ATOM   2189 H  HB2  A GLU   A 1 104 ? 24.209 -3.256  -11.582 0.70 27.60 ?  104 GLU   A HB2  1 
ATOM   2190 H  HB2  B GLU   A 1 104 ? 24.354 -3.714  -11.660 0.30 23.22 ?  104 GLU   A HB2  1 
ATOM   2191 H  HB3  A GLU   A 1 104 ? 25.434 -4.270  -11.664 0.70 27.60 ?  104 GLU   A HB3  1 
ATOM   2192 H  HB3  B GLU   A 1 104 ? 25.794 -4.360  -11.851 0.30 23.22 ?  104 GLU   A HB3  1 
ATOM   2193 H  HG2  A GLU   A 1 104 ? 26.787 -2.702  -12.575 0.70 26.29 ?  104 GLU   A HG2  1 
ATOM   2194 H  HG2  B GLU   A 1 104 ? 26.460 -2.434  -13.037 0.30 23.42 ?  104 GLU   A HG2  1 
ATOM   2195 H  HG3  A GLU   A 1 104 ? 25.569 -1.740  -12.897 0.70 26.29 ?  104 GLU   A HG3  1 
ATOM   2196 H  HG3  B GLU   A 1 104 ? 25.044 -1.787  -12.735 0.30 23.42 ?  104 GLU   A HG3  1 
ATOM   2197 N  N    A ASP   A 1 105 ? 24.599 -6.445  -13.420 0.70 25.70 ?  105 ASP   A N    1 
ATOM   2198 N  N    B ASP   A 1 105 ? 24.754 -6.804  -13.619 0.30 21.80 ?  105 ASP   A N    1 
ATOM   2199 C  CA   A ASP   A 1 105 ? 24.105 -7.811  -13.571 0.70 26.71 ?  105 ASP   A CA   1 
ATOM   2200 C  CA   B ASP   A 1 105 ? 24.231 -8.166  -13.636 0.30 23.26 ?  105 ASP   A CA   1 
ATOM   2201 C  C    A ASP   A 1 105 ? 23.424 -8.284  -12.290 0.70 24.20 ?  105 ASP   A C    1 
ATOM   2202 C  C    B ASP   A 1 105 ? 23.508 -8.492  -12.337 0.30 23.00 ?  105 ASP   A C    1 
ATOM   2203 O  O    A ASP   A 1 105 ? 24.059 -8.368  -11.235 0.70 22.09 ?  105 ASP   A O    1 
ATOM   2204 O  O    B ASP   A 1 105 ? 24.110 -8.482  -11.259 0.30 22.22 ?  105 ASP   A O    1 
ATOM   2205 C  CB   A ASP   A 1 105 ? 25.283 -8.721  -13.915 0.70 29.76 ?  105 ASP   A CB   1 
ATOM   2206 C  CB   B ASP   A 1 105 ? 25.400 -9.129  -13.842 0.30 24.98 ?  105 ASP   A CB   1 
ATOM   2207 C  CG   A ASP   A 1 105 ? 24.869 -10.151 -14.164 0.70 32.34 ?  105 ASP   A CG   1 
ATOM   2208 C  CG   B ASP   A 1 105 ? 24.965 -10.580 -13.948 0.30 26.50 ?  105 ASP   A CG   1 
ATOM   2209 O  OD1  A ASP   A 1 105 ? 23.653 -10.412 -14.250 0.70 32.99 ?  105 ASP   A OD1  1 
ATOM   2210 O  OD1  B ASP   A 1 105 ? 23.746 -10.846 -13.992 0.30 26.71 ?  105 ASP   A OD1  1 
ATOM   2211 O  OD2  A ASP   A 1 105 ? 25.768 -11.013 -14.278 0.70 33.65 -1 105 ASP   A OD2  1 
ATOM   2212 O  OD2  B ASP   A 1 105 ? 25.854 -11.459 -13.981 0.30 27.44 -1 105 ASP   A OD2  1 
ATOM   2213 H  H    A ASP   A 1 105 ? 25.457 -6.393  -13.365 0.70 30.82 ?  105 ASP   A H    1 
ATOM   2214 H  H    B ASP   A 1 105 ? 25.592 -6.754  -13.779 0.30 26.14 ?  105 ASP   A H    1 
ATOM   2215 H  HA   A ASP   A 1 105 ? 23.464 -7.851  -14.298 0.70 32.04 ?  105 ASP   A HA   1 
ATOM   2216 H  HA   B ASP   A 1 105 ? 23.603 -8.264  -14.369 0.30 27.90 ?  105 ASP   A HA   1 
ATOM   2217 H  HB2  A ASP   A 1 105 ? 25.713 -8.396  -14.722 0.70 35.69 ?  105 ASP   A HB2  1 
ATOM   2218 H  HB2  B ASP   A 1 105 ? 25.865 -8.881  -14.657 0.30 29.95 ?  105 ASP   A HB2  1 
ATOM   2219 H  HB3  A ASP   A 1 105 ? 25.914 -8.716  -13.179 0.70 35.69 ?  105 ASP   A HB3  1 
ATOM   2220 H  HB3  B ASP   A 1 105 ? 25.999 -9.060  -13.084 0.30 29.95 ?  105 ASP   A HB3  1 
ATOM   2221 N  N    A ILE   A 1 106 ? 22.135 -8.624  -12.388 0.70 23.86 ?  106 ILE   A N    1 
ATOM   2222 N  N    B ILE   A 1 106 ? 22.214 -8.804  -12.444 0.30 23.38 ?  106 ILE   A N    1 
ATOM   2223 C  CA   A ILE   A 1 106 ? 21.374 -9.040  -11.215 0.70 23.22 ?  106 ILE   A CA   1 
ATOM   2224 C  CA   B ILE   A 1 106 ? 21.434 -9.141  -11.260 0.30 23.82 ?  106 ILE   A CA   1 
ATOM   2225 C  C    A ILE   A 1 106 ? 21.918 -10.324 -10.611 0.70 22.05 ?  106 ILE   A C    1 
ATOM   2226 C  C    B ILE   A 1 106 ? 21.932 -10.422 -10.609 0.30 23.55 ?  106 ILE   A C    1 
ATOM   2227 O  O    A ILE   A 1 106 ? 21.716 -10.572 -9.418  0.70 21.07 ?  106 ILE   A O    1 
ATOM   2228 O  O    B ILE   A 1 106 ? 21.692 -10.642 -9.417  0.30 23.33 ?  106 ILE   A O    1 
ATOM   2229 C  CB   A ILE   A 1 106 ? 19.868 -9.144  -11.550 0.70 24.34 ?  106 ILE   A CB   1 
ATOM   2230 C  CB   B ILE   A 1 106 ? 19.925 -9.202  -11.586 0.30 24.74 ?  106 ILE   A CB   1 
ATOM   2231 C  CG1  A ILE   A 1 106 ? 19.029 -9.258  -10.274 0.70 24.68 ?  106 ILE   A CG1  1 
ATOM   2232 C  CG1  B ILE   A 1 106 ? 19.095 -9.120  -10.302 0.30 25.21 ?  106 ILE   A CG1  1 
ATOM   2233 C  CG2  A ILE   A 1 106 ? 19.597 -10.336 -12.447 0.70 25.02 ?  106 ILE   A CG2  1 
ATOM   2234 C  CG2  B ILE   A 1 106 ? 19.588 -10.478 -12.334 0.30 25.02 ?  106 ILE   A CG2  1 
ATOM   2235 C  CD1  A ILE   A 1 106 ? 19.098 -8.040  -9.380  0.70 24.93 ?  106 ILE   A CD1  1 
ATOM   2236 C  CD1  B ILE   A 1 106 ? 19.340 -7.865  -9.488  0.30 25.47 ?  106 ILE   A CD1  1 
ATOM   2237 H  H    A ILE   A 1 106 ? 21.687 -8.616  -13.118 0.70 28.61 ?  106 ILE   A H    1 
ATOM   2238 H  H    B ILE   A 1 106 ? 21.774 -8.817  -13.182 0.30 28.05 ?  106 ILE   A H    1 
ATOM   2239 H  HA   A ILE   A 1 106 ? 21.476 -8.360  -10.539 0.70 27.85 ?  106 ILE   A HA   1 
ATOM   2240 H  HA   B ILE   A 1 106 ? 21.566 -8.433  -10.618 0.30 28.57 ?  106 ILE   A HA   1 
ATOM   2241 H  HB   A ILE   A 1 106 ? 19.605 -8.337  -12.020 0.70 29.19 ?  106 ILE   A HB   1 
ATOM   2242 H  HB   B ILE   A 1 106 ? 19.699 -8.444  -12.148 0.30 29.68 ?  106 ILE   A HB   1 
ATOM   2243 H  HG12 A ILE   A 1 106 ? 18.101 -9.385  -10.524 0.70 29.60 ?  106 ILE   A HG12 1 
ATOM   2244 H  HG12 B ILE   A 1 106 ? 18.154 -9.138  -10.537 0.30 30.23 ?  106 ILE   A HG12 1 
ATOM   2245 H  HG13 A ILE   A 1 106 ? 19.337 -10.020 -9.761  0.70 29.60 ?  106 ILE   A HG13 1 
ATOM   2246 H  HG13 B ILE   A 1 106 ? 19.309 -9.882  -9.742  0.30 30.23 ?  106 ILE   A HG13 1 
ATOM   2247 H  HG21 A ILE   A 1 106 ? 18.699 -10.259 -12.803 0.70 30.01 ?  106 ILE   A HG21 1 
ATOM   2248 H  HG21 B ILE   A 1 106 ? 18.710 -10.385 -12.734 0.30 30.01 ?  106 ILE   A HG21 1 
ATOM   2249 H  HG22 A ILE   A 1 106 ? 20.244 -10.337 -13.167 0.70 30.01 ?  106 ILE   A HG22 1 
ATOM   2250 H  HG22 B ILE   A 1 106 ? 20.254 -10.622 -13.022 0.30 30.01 ?  106 ILE   A HG22 1 
ATOM   2251 H  HG23 A ILE   A 1 106 ? 19.678 -11.147 -11.923 0.70 30.01 ?  106 ILE   A HG23 1 
ATOM   2252 H  HG23 B ILE   A 1 106 ? 19.590 -11.220 -11.709 0.30 30.01 ?  106 ILE   A HG23 1 
ATOM   2253 H  HD11 A ILE   A 1 106 ? 18.388 -8.092  -8.723  0.70 29.90 ?  106 ILE   A HD11 1 
ATOM   2254 H  HD11 B ILE   A 1 106 ? 18.586 -7.721  -8.899  0.30 30.54 ?  106 ILE   A HD11 1 
ATOM   2255 H  HD12 A ILE   A 1 106 ? 19.960 -8.022  -8.933  0.70 29.90 ?  106 ILE   A HD12 1 
ATOM   2256 H  HD12 B ILE   A 1 106 ? 20.150 -7.980  -8.965  0.30 30.54 ?  106 ILE   A HD12 1 
ATOM   2257 H  HD13 A ILE   A 1 106 ? 18.989 -7.243  -9.922  0.70 29.90 ?  106 ILE   A HD13 1 
ATOM   2258 H  HD13 B ILE   A 1 106 ? 19.439 -7.112  -10.092 0.30 30.54 ?  106 ILE   A HD13 1 
ATOM   2259 N  N    A GLN   A 1 107 ? 22.623 -11.144 -11.402 0.70 22.73 ?  107 GLN   A N    1 
ATOM   2260 N  N    B GLN   A 1 107 ? 22.630 -11.277 -11.363 0.30 23.60 ?  107 GLN   A N    1 
ATOM   2261 C  CA   A GLN   A 1 107 ? 23.236 -12.358 -10.871 0.70 25.07 ?  107 GLN   A CA   1 
ATOM   2262 C  CA   B GLN   A 1 107 ? 23.247 -12.454 -10.764 0.30 24.11 ?  107 GLN   A CA   1 
ATOM   2263 C  C    A GLN   A 1 107 ? 24.208 -12.049 -9.739  0.70 22.60 ?  107 GLN   A C    1 
ATOM   2264 C  C    B GLN   A 1 107 ? 24.267 -12.077 -9.700  0.30 21.86 ?  107 GLN   A C    1 
ATOM   2265 O  O    A GLN   A 1 107 ? 24.423 -12.897 -8.866  0.70 23.84 ?  107 GLN   A O    1 
ATOM   2266 O  O    B GLN   A 1 107 ? 24.595 -12.911 -8.848  0.30 22.37 ?  107 GLN   A O    1 
ATOM   2267 C  CB   A GLN   A 1 107 ? 23.942 -13.121 -12.000 0.70 29.47 ?  107 GLN   A CB   1 
ATOM   2268 C  CB   B GLN   A 1 107 ? 23.898 -13.319 -11.846 0.30 26.67 ?  107 GLN   A CB   1 
ATOM   2269 C  CG   A GLN   A 1 107 ? 23.070 -13.350 -13.232 0.70 34.00 ?  107 GLN   A CG   1 
ATOM   2270 C  CG   B GLN   A 1 107 ? 22.915 -13.864 -12.871 0.30 29.18 ?  107 GLN   A CG   1 
ATOM   2271 C  CD   A GLN   A 1 107 ? 21.787 -14.093 -12.911 0.70 37.85 ?  107 GLN   A CD   1 
ATOM   2272 C  CD   B GLN   A 1 107 ? 21.838 -14.727 -12.242 0.30 31.34 ?  107 GLN   A CD   1 
ATOM   2273 O  OE1  A GLN   A 1 107 ? 21.811 -15.154 -12.288 0.70 39.16 ?  107 GLN   A OE1  1 
ATOM   2274 O  OE1  B GLN   A 1 107 ? 22.117 -15.551 -11.370 0.30 32.04 ?  107 GLN   A OE1  1 
ATOM   2275 N  NE2  A GLN   A 1 107 ? 20.658 -13.533 -13.330 0.70 38.85 ?  107 GLN   A NE2  1 
ATOM   2276 N  NE2  B GLN   A 1 107 ? 20.597 -14.536 -12.677 0.30 31.93 ?  107 GLN   A NE2  1 
ATOM   2277 H  H    A GLN   A 1 107 ? 22.764 -11.016 -12.240 0.70 27.26 ?  107 GLN   A H    1 
ATOM   2278 H  H    B GLN   A 1 107 ? 22.756 -11.199 -12.209 0.30 28.30 ?  107 GLN   A H    1 
ATOM   2279 H  HA   A GLN   A 1 107 ? 22.550 -12.937 -10.515 0.70 30.07 ?  107 GLN   A HA   1 
ATOM   2280 H  HA   B GLN   A 1 107 ? 22.560 -12.984 -10.337 0.30 28.92 ?  107 GLN   A HA   1 
ATOM   2281 H  HB2  A GLN   A 1 107 ? 24.723 -12.620 -12.286 0.70 35.35 ?  107 GLN   A HB2  1 
ATOM   2282 H  HB2  B GLN   A 1 107 ? 24.555 -12.788 -12.322 0.30 31.99 ?  107 GLN   A HB2  1 
ATOM   2283 H  HB3  A GLN   A 1 107 ? 24.216 -13.994 -11.674 0.70 35.35 ?  107 GLN   A HB3  1 
ATOM   2284 H  HB3  B GLN   A 1 107 ? 24.332 -14.078 -11.424 0.30 31.99 ?  107 GLN   A HB3  1 
ATOM   2285 H  HG2  A GLN   A 1 107 ? 22.830 -12.494 -13.621 0.70 40.79 ?  107 GLN   A HG2  1 
ATOM   2286 H  HG2  B GLN   A 1 107 ? 22.481 -13.121 -13.319 0.30 35.00 ?  107 GLN   A HG2  1 
ATOM   2287 H  HG3  A GLN   A 1 107 ? 23.567 -13.875 -13.879 0.70 40.79 ?  107 GLN   A HG3  1 
ATOM   2288 H  HG3  B GLN   A 1 107 ? 23.395 -14.407 -13.516 0.30 35.00 ?  107 GLN   A HG3  1 
ATOM   2289 H  HE21 A GLN   A 1 107 ? 20.679 -12.790 -13.762 0.70 46.61 ?  107 GLN   A HE21 1 
ATOM   2290 H  HE21 B GLN   A 1 107 ? 20.441 -13.949 -13.286 0.30 38.30 ?  107 GLN   A HE21 1 
ATOM   2291 H  HE22 A GLN   A 1 107 ? 19.905 -13.917 -13.170 0.70 46.61 ?  107 GLN   A HE22 1 
ATOM   2292 H  HE22 B GLN   A 1 107 ? 19.951 -14.999 -12.350 0.30 38.30 ?  107 GLN   A HE22 1 
ATOM   2293 N  N    . LEU   A 1 108 ? 24.769 -10.839 -9.717  1.00 19.29 ?  108 LEU   A N    1 
ATOM   2294 C  CA   . LEU   A 1 108 ? 25.681 -10.414 -8.667  1.00 16.28 ?  108 LEU   A CA   1 
ATOM   2295 C  C    . LEU   A 1 108 ? 24.980 -10.241 -7.328  1.00 14.16 ?  108 LEU   A C    1 
ATOM   2296 O  O    . LEU   A 1 108 ? 25.663 -10.084 -6.313  1.00 14.42 ?  108 LEU   A O    1 
ATOM   2297 C  CB   . LEU   A 1 108 ? 26.405 -9.121  -9.074  1.00 16.00 ?  108 LEU   A CB   1 
ATOM   2298 C  CG   . LEU   A 1 108 ? 27.402 -9.321  -10.218 1.00 17.52 ?  108 LEU   A CG   1 
ATOM   2299 C  CD1  . LEU   A 1 108 ? 27.870 -7.990  -10.789 1.00 18.40 ?  108 LEU   A CD1  1 
ATOM   2300 C  CD2  . LEU   A 1 108 ? 28.598 -10.141 -9.754  1.00 19.31 ?  108 LEU   A CD2  1 
ATOM   2301 H  H    A LEU   A 1 108 ? 24.623 -10.238 -10.308 0.70 23.13 ?  108 LEU   A H    1 
ATOM   2302 H  H    B LEU   A 1 108 ? 24.604 -10.250 -10.315 0.30 23.13 ?  108 LEU   A H    1 
ATOM   2303 H  HA   . LEU   A 1 108 ? 26.353 -11.098 -8.544  1.00 19.52 ?  108 LEU   A HA   1 
ATOM   2304 H  HB2  . LEU   A 1 108 ? 25.747 -8.470  -9.364  1.00 19.18 ?  108 LEU   A HB2  1 
ATOM   2305 H  HB3  . LEU   A 1 108 ? 26.892 -8.780  -8.309  1.00 19.18 ?  108 LEU   A HB3  1 
ATOM   2306 H  HG   . LEU   A 1 108 ? 26.968 -9.816  -10.931 1.00 21.01 ?  108 LEU   A HG   1 
ATOM   2307 H  HD11 . LEU   A 1 108 ? 28.483 -8.161  -11.525 1.00 22.06 ?  108 LEU   A HD11 1 
ATOM   2308 H  HD12 . LEU   A 1 108 ? 27.102 -7.496  -11.109 1.00 22.06 ?  108 LEU   A HD12 1 
ATOM   2309 H  HD13 . LEU   A 1 108 ? 28.324 -7.490  -10.094 1.00 22.06 ?  108 LEU   A HD13 1 
ATOM   2310 H  HD21 . LEU   A 1 108 ? 29.285 -10.107 -10.435 1.00 23.15 ?  108 LEU   A HD21 1 
ATOM   2311 H  HD22 . LEU   A 1 108 ? 28.932 -9.763  -8.925  1.00 23.15 ?  108 LEU   A HD22 1 
ATOM   2312 H  HD23 . LEU   A 1 108 ? 28.316 -11.057 -9.610  1.00 23.15 ?  108 LEU   A HD23 1 
ATOM   2313 N  N    . LEU   A 1 109 ? 23.646 -10.293 -7.289  1.00 13.42 ?  109 LEU   A N    1 
ATOM   2314 C  CA   . LEU   A 1 109 ? 22.950 -10.166 -6.015  1.00 12.78 ?  109 LEU   A CA   1 
ATOM   2315 C  C    . LEU   A 1 109 ? 23.292 -11.320 -5.079  1.00 12.18 ?  109 LEU   A C    1 
ATOM   2316 O  O    . LEU   A 1 109 ? 23.429 -11.123 -3.868  1.00 12.59 ?  109 LEU   A O    1 
ATOM   2317 C  CB   . LEU   A 1 109 ? 21.446 -10.086 -6.261  1.00 13.69 ?  109 LEU   A CB   1 
ATOM   2318 C  CG   . LEU   A 1 109 ? 20.551 -9.786  -5.060  1.00 13.80 ?  109 LEU   A CG   1 
ATOM   2319 C  CD1  . LEU   A 1 109 ? 21.007 -8.522  -4.353  1.00 14.00 ?  109 LEU   A CD1  1 
ATOM   2320 C  CD2  . LEU   A 1 109 ? 19.100 -9.654  -5.502  1.00 14.54 ?  109 LEU   A CD2  1 
ATOM   2321 H  H    . LEU   A 1 109 ? 23.131 -10.399 -7.969  1.00 16.09 ?  109 LEU   A H    1 
ATOM   2322 H  HA   . LEU   A 1 109 ? 23.232 -9.342  -5.585  1.00 15.32 ?  109 LEU   A HA   1 
ATOM   2323 H  HB2  . LEU   A 1 109 ? 21.287 -9.384  -6.911  1.00 16.41 ?  109 LEU   A HB2  1 
ATOM   2324 H  HB3  . LEU   A 1 109 ? 21.155 -10.933 -6.624  1.00 16.41 ?  109 LEU   A HB3  1 
ATOM   2325 H  HG   . LEU   A 1 109 ? 20.605 -10.518 -4.429  1.00 16.54 ?  109 LEU   A HG   1 
ATOM   2326 H  HD11 . LEU   A 1 109 ? 20.329 -8.248  -3.716  1.00 16.78 ?  109 LEU   A HD11 1 
ATOM   2327 H  HD12 . LEU   A 1 109 ? 21.842 -8.697  -3.892  1.00 16.78 ?  109 LEU   A HD12 1 
ATOM   2328 H  HD13 . LEU   A 1 109 ? 21.137 -7.817  -5.014  1.00 16.78 ?  109 LEU   A HD13 1 
ATOM   2329 H  HD21 . LEU   A 1 109 ? 18.560 -9.373  -4.745  1.00 17.44 ?  109 LEU   A HD21 1 
ATOM   2330 H  HD22 . LEU   A 1 109 ? 19.040 -8.995  -6.211  1.00 17.44 ?  109 LEU   A HD22 1 
ATOM   2331 H  HD23 . LEU   A 1 109 ? 18.787 -10.516 -5.826  1.00 17.44 ?  109 LEU   A HD23 1 
ATOM   2332 N  N    . LYS   A 1 110 ? 23.434 -12.535 -5.613  1.00 12.05 ?  110 LYS   A N    1 
ATOM   2333 C  CA   . LYS   A 1 110 ? 23.809 -13.653 -4.756  1.00 12.00 ?  110 LYS   A CA   1 
ATOM   2334 C  C    . LYS   A 1 110 ? 25.189 -13.426 -4.147  1.00 11.55 ?  110 LYS   A C    1 
ATOM   2335 O  O    . LYS   A 1 110 ? 25.386 -13.626 -2.946  1.00 11.87 ?  110 LYS   A O    1 
ATOM   2336 C  CB   . LYS   A 1 110 ? 23.737 -14.975 -5.523  1.00 12.85 ?  110 LYS   A CB   1 
ATOM   2337 C  CG   . LYS   A 1 110 ? 23.928 -16.192 -4.611  1.00 13.37 ?  110 LYS   A CG   1 
ATOM   2338 C  CD   . LYS   A 1 110 ? 23.702 -17.520 -5.316  1.00 14.02 ?  110 LYS   A CD   1 
ATOM   2339 C  CE   . LYS   A 1 110 ? 23.813 -18.694 -4.352  1.00 14.62 ?  110 LYS   A CE   1 
ATOM   2340 N  NZ   . LYS   A 1 110 ? 22.631 -18.818 -3.463  1.00 15.02 ?  110 LYS   A NZ   1 
ATOM   2341 H  H    . LYS   A 1 110 ? 23.326 -12.729 -6.440  1.00 14.44 ?  110 LYS   A H    1 
ATOM   2342 H  HA   . LYS   A 1 110 ? 23.171 -13.708 -4.024  1.00 14.38 ?  110 LYS   A HA   1 
ATOM   2343 H  HB2  . LYS   A 1 110 ? 22.866 -15.053 -5.944  1.00 15.41 ?  110 LYS   A HB2  1 
ATOM   2344 H  HB3  . LYS   A 1 110 ? 24.436 -14.993 -6.193  1.00 15.41 ?  110 LYS   A HB3  1 
ATOM   2345 H  HG2  . LYS   A 1 110 ? 24.833 -16.187 -4.263  1.00 16.02 ?  110 LYS   A HG2  1 
ATOM   2346 H  HG3  . LYS   A 1 110 ? 23.295 -16.136 -3.876  1.00 16.02 ?  110 LYS   A HG3  1 
ATOM   2347 H  HD2  . LYS   A 1 110 ? 22.820 -17.533 -5.705  1.00 16.81 ?  110 LYS   A HD2  1 
ATOM   2348 H  HD3  . LYS   A 1 110 ? 24.380 -17.633 -6.003  1.00 16.81 ?  110 LYS   A HD3  1 
ATOM   2349 H  HE2  . LYS   A 1 110 ? 23.895 -19.518 -4.858  1.00 17.52 ?  110 LYS   A HE2  1 
ATOM   2350 H  HE3  . LYS   A 1 110 ? 24.599 -18.575 -3.789  1.00 17.52 ?  110 LYS   A HE3  1 
ATOM   2351 H  HZ1  . LYS   A 1 110 ? 22.726 -19.508 -2.915  1.00 18.00 ?  110 LYS   A HZ1  1 
ATOM   2352 H  HZ2  . LYS   A 1 110 ? 22.536 -18.073 -2.978  1.00 18.00 ?  110 LYS   A HZ2  1 
ATOM   2353 H  HZ3  . LYS   A 1 110 ? 21.894 -18.933 -3.953  1.00 18.00 ?  110 LYS   A HZ3  1 
ATOM   2354 N  N    . SER   A 1 111 ? 26.154 -12.994 -4.965  1.00 11.82 ?  111 SER   A N    1 
ATOM   2355 C  CA   . SER   A 1 111 ? 27.484 -12.683 -4.449  1.00 11.89 ?  111 SER   A CA   1 
ATOM   2356 C  C    . SER   A 1 111 ? 27.416 -11.637 -3.345  1.00 11.72 ?  111 SER   A C    1 
ATOM   2357 O  O    . SER   A 1 111 ? 28.113 -11.742 -2.330  1.00 12.13 ?  111 SER   A O    1 
ATOM   2358 C  CB   . SER   A 1 111 ? 28.376 -12.194 -5.590  1.00 13.19 ?  111 SER   A CB   1 
ATOM   2359 O  OG   . SER   A 1 111 ? 28.469 -13.184 -6.603  1.00 14.97 ?  111 SER   A OG   1 
ATOM   2360 H  H    . SER   A 1 111 ? 26.055 -12.877 -5.809  1.00 14.17 ?  111 SER   A H    1 
ATOM   2361 H  HA   . SER   A 1 111 ? 27.876 -13.489 -4.083  1.00 14.25 ?  111 SER   A HA   1 
ATOM   2362 H  HB2  . SER   A 1 111 ? 27.985 -11.397 -5.980  1.00 15.82 ?  111 SER   A HB2  1 
ATOM   2363 H  HB3  . SER   A 1 111 ? 29.257 -11.998 -5.240  1.00 15.82 ?  111 SER   A HB3  1 
ATOM   2364 H  HG   . SER   A 1 111 ? 28.983 -12.914 -7.219  1.00 17.95 ?  111 SER   A HG   1 
ATOM   2365 N  N    . ALA   A 1 112 ? 26.577 -10.615 -3.527  1.00 11.77 ?  112 ALA   A N    1 
ATOM   2366 C  CA   . ALA   A 1 112 ? 26.430 -9.578  -2.509  1.00 11.66 ?  112 ALA   A CA   1 
ATOM   2367 C  C    . ALA   A 1 112 ? 25.948 -10.176 -1.188  1.00 11.36 ?  112 ALA   A C    1 
ATOM   2368 O  O    . ALA   A 1 112 ? 26.490 -9.877  -0.117  1.00 11.79 ?  112 ALA   A O    1 
ATOM   2369 C  CB   . ALA   A 1 112 ? 25.467 -8.495  -3.008  1.00 11.72 ?  112 ALA   A CB   1 
ATOM   2370 H  H    . ALA   A 1 112 ? 26.088 -10.498 -4.224  1.00 14.10 ?  112 ALA   A H    1 
ATOM   2371 H  HA   . ALA   A 1 112 ? 27.292 -9.156  -2.355  1.00 13.97 ?  112 ALA   A HA   1 
ATOM   2372 H  HB1  . ALA   A 1 112 ? 25.391 -7.797  -2.331  1.00 14.05 ?  112 ALA   A HB1  1 
ATOM   2373 H  HB2  . ALA   A 1 112 ? 25.809 -8.112  -3.831  1.00 14.05 ?  112 ALA   A HB2  1 
ATOM   2374 H  HB3  . ALA   A 1 112 ? 24.594 -8.890  -3.166  1.00 14.05 ?  112 ALA   A HB3  1 
ATOM   2375 N  N    . TYR   A 1 113 ? 24.912 -11.022 -1.239  1.00 11.50 ?  113 TYR   A N    1 
ATOM   2376 C  CA   . TYR   A 1 113 ? 24.396 -11.620 -0.011  1.00 11.16 ?  113 TYR   A CA   1 
ATOM   2377 C  C    . TYR   A 1 113 ? 25.396 -12.575 0.637   1.00 11.03 ?  113 TYR   A C    1 
ATOM   2378 O  O    . TYR   A 1 113 ? 25.357 -12.759 1.857   1.00 11.63 ?  113 TYR   A O    1 
ATOM   2379 C  CB   . TYR   A 1 113 ? 23.076 -12.345 -0.280  1.00 11.76 ?  113 TYR   A CB   1 
ATOM   2380 C  CG   . TYR   A 1 113 ? 21.864 -11.444 -0.198  1.00 11.45 ?  113 TYR   A CG   1 
ATOM   2381 C  CD1  . TYR   A 1 113 ? 21.502 -10.846 1.004   1.00 11.56 ?  113 TYR   A CD1  1 
ATOM   2382 C  CD2  . TYR   A 1 113 ? 21.056 -11.224 -1.305  1.00 11.54 ?  113 TYR   A CD2  1 
ATOM   2383 C  CE1  . TYR   A 1 113 ? 20.379 -10.037 1.097   1.00 11.98 ?  113 TYR   A CE1  1 
ATOM   2384 C  CE2  . TYR   A 1 113 ? 19.910 -10.414 -1.220  1.00 12.14 ?  113 TYR   A CE2  1 
ATOM   2385 C  CZ   . TYR   A 1 113 ? 19.582 -9.835  -0.012  1.00 11.93 ?  113 TYR   A CZ   1 
ATOM   2386 O  OH   . TYR   A 1 113 ? 18.463 -9.035  0.101   1.00 12.52 ?  113 TYR   A OH   1 
ATOM   2387 H  H    . TYR   A 1 113 ? 24.510 -11.259 -1.961  1.00 13.78 ?  113 TYR   A H    1 
ATOM   2388 H  HA   . TYR   A 1 113 ? 24.222 -10.912 0.623   1.00 13.38 ?  113 TYR   A HA   1 
ATOM   2389 H  HB2  . TYR   A 1 113 ? 23.098 -12.721 -1.173  1.00 14.09 ?  113 TYR   A HB2  1 
ATOM   2390 H  HB3  . TYR   A 1 113 ? 22.966 -13.050 0.374   1.00 14.09 ?  113 TYR   A HB3  1 
ATOM   2391 H  HD1  . TYR   A 1 113 ? 22.032 -10.988 1.758   1.00 13.86 ?  113 TYR   A HD1  1 
ATOM   2392 H  HD2  . TYR   A 1 113 ? 21.267 -11.627 -2.114  1.00 13.84 ?  113 TYR   A HD2  1 
ATOM   2393 H  HE1  . TYR   A 1 113 ? 20.158 -9.647  1.910   1.00 14.35 ?  113 TYR   A HE1  1 
ATOM   2394 H  HE2  . TYR   A 1 113 ? 19.370 -10.273 -1.966  1.00 14.55 ?  113 TYR   A HE2  1 
ATOM   2395 H  HH   . TYR   A 1 113 ? 18.073 -8.998  -0.647  1.00 15.00 ?  113 TYR   A HH   1 
ATOM   2396 N  N    . GLU   A 1 114 ? 26.298 -13.191 -0.144  1.00 11.32 ?  114 GLU   A N    1 
ATOM   2397 C  CA   . GLU   A 1 114 ? 27.294 -14.084 0.454   1.00 11.64 ?  114 GLU   A CA   1 
ATOM   2398 C  C    . GLU   A 1 114 ? 28.138 -13.371 1.505   1.00 11.58 ?  114 GLU   A C    1 
ATOM   2399 O  O    . GLU   A 1 114 ? 28.616 -14.004 2.455   1.00 12.01 ?  114 GLU   A O    1 
ATOM   2400 C  CB   . GLU   A 1 114 ? 28.167 -14.727 -0.634  1.00 11.82 ?  114 GLU   A CB   1 
ATOM   2401 C  CG   . GLU   A 1 114 ? 27.398 -15.777 -1.420  1.00 12.30 ?  114 GLU   A CG   1 
ATOM   2402 C  CD   . GLU   A 1 114 ? 28.110 -16.317 -2.652  1.00 12.76 ?  114 GLU   A CD   1 
ATOM   2403 O  OE1  . GLU   A 1 114 ? 29.070 -15.690 -3.151  1.00 12.86 ?  114 GLU   A OE1  1 
ATOM   2404 O  OE2  . GLU   A 1 114 ? 27.671 -17.386 -3.140  1.00 13.87 -1 114 GLU   A OE2  1 
ATOM   2405 H  H    . GLU   A 1 114 ? 26.353 -13.102 -1.005  1.00 13.57 ?  114 GLU   A H    1 
ATOM   2406 H  HA   . GLU   A 1 114 ? 26.820 -14.798 0.899   1.00 13.95 ?  114 GLU   A HA   1 
ATOM   2407 H  HB2  . GLU   A 1 114 ? 28.463 -14.045 -1.258  1.00 14.17 ?  114 GLU   A HB2  1 
ATOM   2408 H  HB3  . GLU   A 1 114 ? 28.925 -15.160 -0.222  1.00 14.17 ?  114 GLU   A HB3  1 
ATOM   2409 H  HG2  . GLU   A 1 114 ? 27.220 -16.531 -0.840  1.00 14.74 ?  114 GLU   A HG2  1 
ATOM   2410 H  HG3  . GLU   A 1 114 ? 26.555 -15.391 -1.715  1.00 14.74 ?  114 GLU   A HG3  1 
ATOM   2411 N  N    . ASN   A 1 115 ? 28.320 -12.054 1.372   1.00 11.26 ?  115 ASN   A N    1 
ATOM   2412 C  CA   . ASN   A 1 115 ? 29.086 -11.325 2.379   1.00 11.62 ?  115 ASN   A CA   1 
ATOM   2413 C  C    . ASN   A 1 115 ? 28.469 -11.455 3.767   1.00 11.43 ?  115 ASN   A C    1 
ATOM   2414 O  O    . ASN   A 1 115 ? 29.182 -11.392 4.775   1.00 11.90 ?  115 ASN   A O    1 
ATOM   2415 C  CB   . ASN   A 1 115 ? 29.194 -9.850  2.000   1.00 12.00 ?  115 ASN   A CB   1 
ATOM   2416 C  CG   . ASN   A 1 115 ? 29.998 -9.633  0.741   1.00 12.47 ?  115 ASN   A CG   1 
ATOM   2417 O  OD1  . ASN   A 1 115 ? 31.217 -9.740  0.756   1.00 16.04 ?  115 ASN   A OD1  1 
ATOM   2418 N  ND2  . ASN   A 1 115 ? 29.326 -9.333  -0.354  1.00 12.20 ?  115 ASN   A ND2  1 
ATOM   2419 H  H    . ASN   A 1 115 ? 28.011 -11.567 0.729   1.00 13.50 ?  115 ASN   A H    1 
ATOM   2420 H  HA   . ASN   A 1 115 ? 29.977 -11.689 2.420   1.00 13.92 ?  115 ASN   A HA   1 
ATOM   2421 H  HB2  . ASN   A 1 115 ? 28.301 -9.491  1.862   1.00 14.38 ?  115 ASN   A HB2  1 
ATOM   2422 H  HB3  . ASN   A 1 115 ? 29.629 -9.370  2.727   1.00 14.38 ?  115 ASN   A HB3  1 
ATOM   2423 H  HD21 . ASN   A 1 115 ? 29.744 -9.201  -1.093  1.00 14.63 ?  115 ASN   A HD21 1 
ATOM   2424 H  HD22 . ASN   A 1 115 ? 28.467 -9.281  -0.330  1.00 14.63 ?  115 ASN   A HD22 1 
ATOM   2425 N  N    . PHE   A 1 116 ? 27.143 -11.623 3.848   1.00 11.39 ?  116 PHE   A N    1 
ATOM   2426 C  CA   . PHE   A 1 116 ? 26.490 -11.724 5.150   1.00 11.49 ?  116 PHE   A CA   1 
ATOM   2427 C  C    . PHE   A 1 116 ? 26.963 -12.955 5.922   1.00 11.79 ?  116 PHE   A C    1 
ATOM   2428 O  O    . PHE   A 1 116 ? 26.892 -12.975 7.152   1.00 12.32 ?  116 PHE   A O    1 
ATOM   2429 C  CB   . PHE   A 1 116 ? 24.964 -11.853 5.007   1.00 11.66 ?  116 PHE   A CB   1 
ATOM   2430 C  CG   . PHE   A 1 116 ? 24.213 -10.604 4.539   1.00 11.28 ?  116 PHE   A CG   1 
ATOM   2431 C  CD1  . PHE   A 1 116 ? 24.789 -9.581  3.794   1.00 11.32 ?  116 PHE   A CD1  1 
ATOM   2432 C  CD2  . PHE   A 1 116 ? 22.855 -10.498 4.849   1.00 11.87 ?  116 PHE   A CD2  1 
ATOM   2433 C  CE1  . PHE   A 1 116 ? 24.020 -8.498  3.375   1.00 11.77 ?  116 PHE   A CE1  1 
ATOM   2434 C  CE2  . PHE   A 1 116 ? 22.096 -9.424  4.439   1.00 12.01 ?  116 PHE   A CE2  1 
ATOM   2435 C  CZ   . PHE   A 1 116 ? 22.671 -8.423  3.703   1.00 11.58 ?  116 PHE   A CZ   1 
ATOM   2436 H  H    . PHE   A 1 116 ? 26.604 -11.674 3.173   1.00 13.66 ?  116 PHE   A H    1 
ATOM   2437 H  HA   . PHE   A 1 116 ? 26.684 -10.932 5.677   1.00 13.77 ?  116 PHE   A HA   1 
ATOM   2438 H  HB2  . PHE   A 1 116 ? 24.778 -12.559 4.369   1.00 13.98 ?  116 PHE   A HB2  1 
ATOM   2439 H  HB3  . PHE   A 1 116 ? 24.599 -12.103 5.873   1.00 13.98 ?  116 PHE   A HB3  1 
ATOM   2440 H  HD1  . PHE   A 1 116 ? 25.684 -9.639  3.566   1.00 13.57 ?  116 PHE   A HD1  1 
ATOM   2441 H  HD2  . PHE   A 1 116 ? 22.449 -11.185 5.343   1.00 14.22 ?  116 PHE   A HD2  1 
ATOM   2442 H  HE1  . PHE   A 1 116 ? 24.414 -7.821  2.883   1.00 14.11 ?  116 PHE   A HE1  1 
ATOM   2443 H  HE2  . PHE   A 1 116 ? 21.191 -9.387  4.668   1.00 14.39 ?  116 PHE   A HE2  1 
ATOM   2444 H  HZ   . PHE   A 1 116 ? 22.161 -7.694  3.435   1.00 13.88 ?  116 PHE   A HZ   1 
ATOM   2445 N  N    . ASN   A 1 117 ? 27.410 -14.005 5.221   1.00 11.87 ?  117 ASN   A N    1 
ATOM   2446 C  CA   . ASN   A 1 117 ? 27.780 -15.252 5.885   1.00 12.08 ?  117 ASN   A CA   1 
ATOM   2447 C  C    . ASN   A 1 117 ? 29.036 -15.131 6.730   1.00 12.76 ?  117 ASN   A C    1 
ATOM   2448 O  O    . ASN   A 1 117 ? 29.331 -16.053 7.501   1.00 13.70 ?  117 ASN   A O    1 
ATOM   2449 C  CB   . ASN   A 1 117 ? 27.899 -16.374 4.859   1.00 12.27 ?  117 ASN   A CB   1 
ATOM   2450 C  CG   . ASN   A 1 117 ? 26.546 -16.757 4.316   1.00 12.43 ?  117 ASN   A CG   1 
ATOM   2451 O  OD1  . ASN   A 1 117 ? 25.568 -16.780 5.063   1.00 13.11 ?  117 ASN   A OD1  1 
ATOM   2452 N  ND2  . ASN   A 1 117 ? 26.465 -17.020 3.026   1.00 12.22 ?  117 ASN   A ND2  1 
ATOM   2453 H  H    . ASN   A 1 117 ? 27.488 -14.020 4.359   1.00 14.22 ?  117 ASN   A H    1 
ATOM   2454 H  HA   . ASN   A 1 117 ? 27.052 -15.490 6.482   1.00 14.48 ?  117 ASN   A HA   1 
ATOM   2455 H  HB2  . ASN   A 1 117 ? 28.451 -16.075 4.119   1.00 14.70 ?  117 ASN   A HB2  1 
ATOM   2456 H  HB3  . ASN   A 1 117 ? 28.289 -17.150 5.282   1.00 14.70 ?  117 ASN   A HB3  1 
ATOM   2457 H  HD21 . ASN   A 1 117 ? 25.710 -17.234 2.681   1.00 14.64 ?  117 ASN   A HD21 1 
ATOM   2458 H  HD22 . ASN   A 1 117 ? 27.171 -16.982 2.537   1.00 14.64 ?  117 ASN   A HD22 1 
ATOM   2459 N  N    . GLN   A 1 118 ? 29.766 -14.019 6.617   1.00 12.76 ?  118 GLN   A N    1 
ATOM   2460 C  CA   . GLN   A 1 118 ? 30.943 -13.781 7.441   1.00 13.47 ?  118 GLN   A CA   1 
ATOM   2461 C  C    . GLN   A 1 118 ? 30.595 -13.201 8.806   1.00 13.35 ?  118 GLN   A C    1 
ATOM   2462 O  O    . GLN   A 1 118 ? 31.508 -12.900 9.587   1.00 14.45 ?  118 GLN   A O    1 
ATOM   2463 C  CB   . GLN   A 1 118 ? 31.942 -12.876 6.705   1.00 13.45 ?  118 GLN   A CB   1 
ATOM   2464 C  CG   . GLN   A 1 118 ? 32.403 -13.458 5.380   1.00 13.56 ?  118 GLN   A CG   1 
ATOM   2465 C  CD   . GLN   A 1 118 ? 33.244 -14.719 5.555   1.00 13.97 ?  118 GLN   A CD   1 
ATOM   2466 O  OE1  . GLN   A 1 118 ? 34.116 -14.783 6.433   1.00 14.66 ?  118 GLN   A OE1  1 
ATOM   2467 N  NE2  . GLN   A 1 118 ? 32.995 -15.722 4.711   1.00 14.16 ?  118 GLN   A NE2  1 
ATOM   2468 H  H    . GLN   A 1 118 ? 29.585 -13.373 6.069   1.00 15.29 ?  118 GLN   A H    1 
ATOM   2469 H  HA   . GLN   A 1 118 ? 31.372 -14.637 7.593   1.00 16.15 ?  118 GLN   A HA   1 
ATOM   2470 H  HB2  . GLN   A 1 118 ? 31.522 -12.023 6.532   1.00 16.12 ?  118 GLN   A HB2  1 
ATOM   2471 H  HB3  . GLN   A 1 118 ? 32.722 -12.758 7.269   1.00 16.12 ?  118 GLN   A HB3  1 
ATOM   2472 H  HG2  . GLN   A 1 118 ? 31.627 -13.681 4.840   1.00 16.25 ?  118 GLN   A HG2  1 
ATOM   2473 H  HG3  . GLN   A 1 118 ? 32.946 -12.798 4.918   1.00 16.25 ?  118 GLN   A HG3  1 
ATOM   2474 H  HE21 . GLN   A 1 118 ? 32.372 -15.638 4.112   1.00 16.98 ?  118 GLN   A HE21 1 
ATOM   2475 H  HE22 . GLN   A 1 118 ? 33.433 -16.455 4.766   1.00 16.98 ?  118 GLN   A HE22 1 
ATOM   2476 N  N    . HIS   A 1 119 ? 29.305 -13.047 9.110   1.00 12.87 ?  119 HIS   A N    1 
ATOM   2477 C  CA   . HIS   A 1 119 ? 28.846 -12.436 10.350  1.00 13.23 ?  119 HIS   A CA   1 
ATOM   2478 C  C    . HIS   A 1 119 ? 27.706 -13.259 10.926  1.00 13.60 ?  119 HIS   A C    1 
ATOM   2479 O  O    . HIS   A 1 119 ? 26.762 -13.602 10.209  1.00 13.90 ?  119 HIS   A O    1 
ATOM   2480 C  CB   . HIS   A 1 119 ? 28.391 -11.009 10.068  1.00 13.92 ?  119 HIS   A CB   1 
ATOM   2481 C  CG   . HIS   A 1 119 ? 29.476 -10.198 9.459   1.00 14.93 ?  119 HIS   A CG   1 
ATOM   2482 N  ND1  . HIS   A 1 119 ? 30.443 -9.579  10.218  1.00 17.58 ?  119 HIS   A ND1  1 
ATOM   2483 C  CD2  . HIS   A 1 119 ? 29.820 -10.007 8.166   1.00 15.95 ?  119 HIS   A CD2  1 
ATOM   2484 C  CE1  . HIS   A 1 119 ? 31.312 -8.995  9.414   1.00 17.68 ?  119 HIS   A CE1  1 
ATOM   2485 N  NE2  . HIS   A 1 119 ? 30.964 -9.246  8.164   1.00 17.45 ?  119 HIS   A NE2  1 
ATOM   2486 H  H    . HIS   A 1 119 ? 28.655 -13.313 8.602   1.00 15.43 ?  119 HIS   A H    1 
ATOM   2487 H  HA   . HIS   A 1 119 ? 29.572 -12.419 10.992  1.00 15.86 ?  119 HIS   A HA   1 
ATOM   2488 H  HB2  . HIS   A 1 119 ? 27.640 -11.035 9.453   1.00 16.69 ?  119 HIS   A HB2  1 
ATOM   2489 H  HB3  . HIS   A 1 119 ? 28.128 -10.594 10.902  1.00 16.69 ?  119 HIS   A HB3  1 
ATOM   2490 H  HD2  . HIS   A 1 119 ? 29.365 -10.324 7.415   1.00 19.12 ?  119 HIS   A HD2  1 
ATOM   2491 H  HE1  . HIS   A 1 119 ? 32.046 -8.492  9.680   1.00 21.20 ?  119 HIS   A HE1  1 
ATOM   2492 H  HE2  . HIS   A 1 119 ? 31.372 -8.957  7.462   1.00 20.92 ?  119 HIS   A HE2  1 
ATOM   2493 N  N    . GLU   A 1 120 ? 27.788 -13.559 12.224  1.00 14.68 ?  120 GLU   A N    1 
ATOM   2494 C  CA   . GLU   A 1 120 ? 26.833 -14.489 12.824  1.00 16.97 ?  120 GLU   A CA   1 
ATOM   2495 C  C    . GLU   A 1 120 ? 25.416 -13.928 12.879  1.00 15.30 ?  120 GLU   A C    1 
ATOM   2496 O  O    . GLU   A 1 120 ? 24.446 -14.696 12.766  1.00 15.35 ?  120 GLU   A O    1 
ATOM   2497 C  CB   . GLU   A 1 120 ? 27.301 -14.885 14.226  1.00 22.09 ?  120 GLU   A CB   1 
ATOM   2498 C  CG   . GLU   A 1 120 ? 28.506 -15.812 14.238  1.00 29.77 ?  120 GLU   A CG   1 
ATOM   2499 C  CD   . GLU   A 1 120 ? 28.679 -16.528 15.561  1.00 37.36 ?  120 GLU   A CD   1 
ATOM   2500 O  OE1  . GLU   A 1 120 ? 28.299 -15.955 16.605  1.00 38.89 ?  120 GLU   A OE1  1 
ATOM   2501 O  OE2  . GLU   A 1 120 ? 29.194 -17.666 15.557  1.00 40.71 -1 120 GLU   A OE2  1 
ATOM   2502 H  H    . GLU   A 1 120 ? 28.385 -13.249 12.770  1.00 17.60 ?  120 GLU   A H    1 
ATOM   2503 H  HA   . GLU   A 1 120 ? 26.814 -15.298 12.294  1.00 20.35 ?  120 GLU   A HA   1 
ATOM   2504 H  HB2  . GLU   A 1 120 ? 27.546 -14.090 14.723  1.00 26.49 ?  120 GLU   A HB2  1 
ATOM   2505 H  HB3  . GLU   A 1 120 ? 26.578 -15.347 14.685  1.00 26.49 ?  120 GLU   A HB3  1 
ATOM   2506 H  HG2  . GLU   A 1 120 ? 28.405 -16.477 13.540  1.00 35.71 ?  120 GLU   A HG2  1 
ATOM   2507 H  HG3  . GLU   A 1 120 ? 29.311 -15.295 14.095  1.00 35.71 ?  120 GLU   A HG3  1 
ATOM   2508 N  N    . VAL   A 1 121 ? 25.279 -12.618 13.092  1.00 14.44 ?  121 VAL   A N    1 
ATOM   2509 C  CA   . VAL   A 1 121 ? 23.985 -11.951 13.211  1.00 14.56 ?  121 VAL   A CA   1 
ATOM   2510 C  C    . VAL   A 1 121 ? 24.097 -10.571 12.568  1.00 13.28 ?  121 VAL   A C    1 
ATOM   2511 O  O    . VAL   A 1 121 ? 25.069 -9.846  12.806  1.00 14.01 ?  121 VAL   A O    1 
ATOM   2512 C  CB   . VAL   A 1 121 ? 23.549 -11.800 14.687  1.00 17.60 ?  121 VAL   A CB   1 
ATOM   2513 C  CG1  . VAL   A 1 121 ? 22.155 -11.186 14.776  1.00 18.06 ?  121 VAL   A CG1  1 
ATOM   2514 C  CG2  . VAL   A 1 121 ? 23.581 -13.128 15.426  1.00 19.83 ?  121 VAL   A CG2  1 
ATOM   2515 H  H    . VAL   A 1 121 ? 25.945 -12.075 13.175  1.00 17.31 ?  121 VAL   A H    1 
ATOM   2516 H  HA   . VAL   A 1 121 ? 23.312 -12.467 12.740  1.00 17.45 ?  121 VAL   A HA   1 
ATOM   2517 H  HB   . VAL   A 1 121 ? 24.161 -11.199 15.135  1.00 21.11 ?  121 VAL   A HB   1 
ATOM   2518 H  HG11 . VAL   A 1 121 ? 21.847 -11.231 15.697  1.00 21.65 ?  121 VAL   A HG11 1 
ATOM   2519 H  HG12 . VAL   A 1 121 ? 22.193 -10.262 14.487  1.00 21.65 ?  121 VAL   A HG12 1 
ATOM   2520 H  HG13 . VAL   A 1 121 ? 21.549 -11.688 14.206  1.00 21.65 ?  121 VAL   A HG13 1 
ATOM   2521 H  HG21 . VAL   A 1 121 ? 23.230 -12.999 16.326  1.00 23.78 ?  121 VAL   A HG21 1 
ATOM   2522 H  HG22 . VAL   A 1 121 ? 23.027 -13.771 14.952  1.00 23.78 ?  121 VAL   A HG22 1 
ATOM   2523 H  HG23 . VAL   A 1 121 ? 24.493 -13.446 15.473  1.00 23.78 ?  121 VAL   A HG23 1 
ATOM   2524 N  N    . LEU   A 1 122 ? 23.087 -10.189 11.782  1.00 12.65 ?  122 LEU   A N    1 
ATOM   2525 C  CA   . LEU   A 1 122 ? 23.090 -8.897  11.104  1.00 12.50 ?  122 LEU   A CA   1 
ATOM   2526 C  C    . LEU   A 1 122 ? 21.692 -8.301  11.074  1.00 12.34 ?  122 LEU   A C    1 
ATOM   2527 O  O    . LEU   A 1 122 ? 20.701 -9.020  10.936  1.00 13.14 ?  122 LEU   A O    1 
ATOM   2528 C  CB   . LEU   A 1 122 ? 23.519 -9.000  9.638   1.00 13.68 ?  122 LEU   A CB   1 
ATOM   2529 C  CG   . LEU   A 1 122 ? 24.735 -9.846  9.295   1.00 13.56 ?  122 LEU   A CG   1 
ATOM   2530 C  CD1  . LEU   A 1 122 ? 24.330 -11.291 9.063   1.00 14.66 ?  122 LEU   A CD1  1 
ATOM   2531 C  CD2  . LEU   A 1 122 ? 25.428 -9.276  8.069   1.00 13.20 ?  122 LEU   A CD2  1 
ATOM   2532 H  H    . LEU   A 1 122 ? 22.380 -10.662 11.628  1.00 15.16 ?  122 LEU   A H    1 
ATOM   2533 H  HA   . LEU   A 1 122 ? 23.685 -8.283  11.562  1.00 14.98 ?  122 LEU   A HA   1 
ATOM   2534 H  HB2  . LEU   A 1 122 ? 22.782 -9.367  9.135   1.00 16.40 ?  122 LEU   A HB2  1 
ATOM   2535 H  HB3  . LEU   A 1 122 ? 23.713 -8.107  9.320   1.00 16.40 ?  122 LEU   A HB3  1 
ATOM   2536 H  HG   . LEU   A 1 122 ? 25.373 -9.831  10.030  1.00 16.25 ?  122 LEU   A HG   1 
ATOM   2537 H  HD11 . LEU   A 1 122 ? 25.110 -11.814 8.814   1.00 17.57 ?  122 LEU   A HD11 1 
ATOM   2538 H  HD12 . LEU   A 1 122 ? 23.944 -11.650 9.879   1.00 17.57 ?  122 LEU   A HD12 1 
ATOM   2539 H  HD13 . LEU   A 1 122 ? 23.672 -11.326 8.348   1.00 17.57 ?  122 LEU   A HD13 1 
ATOM   2540 H  HD21 . LEU   A 1 122 ? 26.181 -9.850  7.826   1.00 15.83 ?  122 LEU   A HD21 1 
ATOM   2541 H  HD22 . LEU   A 1 122 ? 24.799 -9.240  7.335   1.00 15.83 ?  122 LEU   A HD22 1 
ATOM   2542 H  HD23 . LEU   A 1 122 ? 25.755 -8.386  8.273   1.00 15.83 ?  122 LEU   A HD23 1 
ATOM   2543 N  N    . LEU   A 1 123 ? 21.633 -6.974  11.170  1.00 12.10 ?  123 LEU   A N    1 
ATOM   2544 C  CA   . LEU   A 1 123 ? 20.465 -6.178  10.802  1.00 11.81 ?  123 LEU   A CA   1 
ATOM   2545 C  C    . LEU   A 1 123 ? 20.704 -5.657  9.393   1.00 11.27 ?  123 LEU   A C    1 
ATOM   2546 O  O    . LEU   A 1 123 ? 21.755 -5.063  9.136   1.00 11.90 ?  123 LEU   A O    1 
ATOM   2547 C  CB   . LEU   A 1 123 ? 20.328 -4.994  11.761  1.00 12.23 ?  123 LEU   A CB   1 
ATOM   2548 C  CG   . LEU   A 1 123 ? 19.274 -3.935  11.426  1.00 12.94 ?  123 LEU   A CG   1 
ATOM   2549 C  CD1  . LEU   A 1 123 ? 17.873 -4.528  11.417  1.00 13.49 ?  123 LEU   A CD1  1 
ATOM   2550 C  CD2  . LEU   A 1 123 ? 19.366 -2.769  12.407  1.00 13.73 ?  123 LEU   A CD2  1 
ATOM   2551 H  H    . LEU   A 1 123 ? 22.291 -6.493  11.448  1.00 14.51 ?  123 LEU   A H    1 
ATOM   2552 H  HA   . LEU   A 1 123 ? 19.661 -6.719  10.822  1.00 14.16 ?  123 LEU   A HA   1 
ATOM   2553 H  HB2  . LEU   A 1 123 ? 20.103 -5.343  12.640  1.00 14.66 ?  123 LEU   A HB2  1 
ATOM   2554 H  HB3  . LEU   A 1 123 ? 21.179 -4.538  11.806  1.00 14.66 ?  123 LEU   A HB3  1 
ATOM   2555 H  HG   . LEU   A 1 123 ? 19.443 -3.581  10.537  1.00 15.51 ?  123 LEU   A HG   1 
ATOM   2556 H  HD11 . LEU   A 1 123 ? 17.227 -3.831  11.230  1.00 16.17 ?  123 LEU   A HD11 1 
ATOM   2557 H  HD12 . LEU   A 1 123 ? 17.823 -5.216  10.732  1.00 16.17 ?  123 LEU   A HD12 1 
ATOM   2558 H  HD13 . LEU   A 1 123 ? 17.690 -4.922  12.288  1.00 16.17 ?  123 LEU   A HD13 1 
ATOM   2559 H  HD21 . LEU   A 1 123 ? 18.690 -2.109  12.183  1.00 16.46 ?  123 LEU   A HD21 1 
ATOM   2560 H  HD22 . LEU   A 1 123 ? 19.211 -3.104  13.307  1.00 16.46 ?  123 LEU   A HD22 1 
ATOM   2561 H  HD23 . LEU   A 1 123 ? 20.248 -2.377  12.348  1.00 16.46 ?  123 LEU   A HD23 1 
ATOM   2562 N  N    . ALA   A 1 124 ? 19.746 -5.854  8.487   1.00 10.80 ?  124 ALA   A N    1 
ATOM   2563 C  CA   . ALA   A 1 124 ? 20.026 -5.572  7.089   1.00 10.98 ?  124 ALA   A CA   1 
ATOM   2564 C  C    . ALA   A 1 124 ? 18.796 -5.112  6.320   1.00 10.71 ?  124 ALA   A C    1 
ATOM   2565 O  O    . ALA   A 1 124 ? 17.661 -5.460  6.683   1.00 11.57 ?  124 ALA   A O    1 
ATOM   2566 C  CB   . ALA   A 1 124 ? 20.606 -6.805  6.386   1.00 11.40 ?  124 ALA   A CB   1 
ATOM   2567 H  H    . ALA   A 1 124 ? 18.948 -6.141  8.653   1.00 12.94 ?  124 ALA   A H    1 
ATOM   2568 H  HA   . ALA   A 1 124 ? 20.695 -4.871  7.059   1.00 13.16 ?  124 ALA   A HA   1 
ATOM   2569 H  HB1  . ALA   A 1 124 ? 20.792 -6.590  5.458   1.00 13.67 ?  124 ALA   A HB1  1 
ATOM   2570 H  HB2  . ALA   A 1 124 ? 21.440 -7.059  6.831   1.00 13.67 ?  124 ALA   A HB2  1 
ATOM   2571 H  HB3  . ALA   A 1 124 ? 19.975 -7.533  6.441   1.00 13.67 ?  124 ALA   A HB3  1 
ATOM   2572 N  N    A PRO   A 1 125 ? 18.996 -4.387  5.220   0.70 10.67 ?  125 PRO   A N    1 
ATOM   2573 N  N    B PRO   A 1 125 ? 18.983 -4.307  5.275   0.30 10.76 ?  125 PRO   A N    1 
ATOM   2574 C  CA   A PRO   A 1 125 ? 17.945 -4.147  4.233   0.70 10.69 ?  125 PRO   A CA   1 
ATOM   2575 C  CA   B PRO   A 1 125 ? 17.871 -3.984  4.381   0.30 10.95 ?  125 PRO   A CA   1 
ATOM   2576 C  C    A PRO   A 1 125 ? 17.989 -5.219  3.149   0.70 10.37 ?  125 PRO   A C    1 
ATOM   2577 C  C    B PRO   A 1 125 ? 17.841 -4.985  3.241   0.30 10.73 ?  125 PRO   A C    1 
ATOM   2578 O  O    A PRO   A 1 125 ? 18.956 -5.977  3.027   0.70 10.71 ?  125 PRO   A O    1 
ATOM   2579 O  O    B PRO   A 1 125 ? 18.728 -5.842  3.156   0.30 11.39 ?  125 PRO   A O    1 
ATOM   2580 C  CB   A PRO   A 1 125 ? 18.394 -2.810  3.631   0.70 10.80 ?  125 PRO   A CB   1 
ATOM   2581 C  CB   B PRO   A 1 125 ? 18.256 -2.593  3.872   0.30 11.09 ?  125 PRO   A CB   1 
ATOM   2582 C  CG   A PRO   A 1 125 ? 19.903 -2.970  3.554   0.70 10.56 ?  125 PRO   A CG   1 
ATOM   2583 C  CG   B PRO   A 1 125 ? 19.753 -2.696  3.740   0.30 11.22 ?  125 PRO   A CG   1 
ATOM   2584 C  CD   A PRO   A 1 125 ? 20.273 -3.778  4.797   0.70 10.93 ?  125 PRO   A CD   1 
ATOM   2585 C  CD   B PRO   A 1 125 ? 20.221 -3.624  4.853   0.30 11.15 ?  125 PRO   A CD   1 
ATOM   2586 H  HA   A PRO   A 1 125 ? 17.066 -4.091  4.637   0.70 12.81 ?  125 PRO   A HA   1 
ATOM   2587 H  HA   B PRO   A 1 125 ? 17.021 -3.956  4.857   0.30 13.13 ?  125 PRO   A HA   1 
ATOM   2588 H  HB2  A PRO   A 1 125 ? 17.999 -2.699  2.748   0.70 12.95 ?  125 PRO   A HB2  1 
ATOM   2589 H  HB2  B PRO   A 1 125 ? 17.838 -2.430  3.012   0.30 13.29 ?  125 PRO   A HB2  1 
ATOM   2590 H  HB3  A PRO   A 1 125 ? 18.139 -2.087  4.221   0.70 12.95 ?  125 PRO   A HB3  1 
ATOM   2591 H  HB3  B PRO   A 1 125 ? 18.002 -1.914  4.519   0.30 13.29 ?  125 PRO   A HB3  1 
ATOM   2592 H  HG2  A PRO   A 1 125 ? 20.140 -3.453  2.743   0.70 12.65 ?  125 PRO   A HG2  1 
ATOM   2593 H  HG2  B PRO   A 1 125 ? 19.974 -3.069  2.873   0.30 13.45 ?  125 PRO   A HG2  1 
ATOM   2594 H  HG3  A PRO   A 1 125 ? 20.321 -2.096  3.566   0.70 12.65 ?  125 PRO   A HG3  1 
ATOM   2595 H  HG3  B PRO   A 1 125 ? 20.148 -1.819  3.841   0.30 13.45 ?  125 PRO   A HG3  1 
ATOM   2596 H  HD2  A PRO   A 1 125 ? 20.930 -4.455  4.571   0.70 13.11 ?  125 PRO   A HD2  1 
ATOM   2597 H  HD2  B PRO   A 1 125 ? 20.863 -4.265  4.507   0.30 13.37 ?  125 PRO   A HD2  1 
ATOM   2598 H  HD3  A PRO   A 1 125 ? 20.604 -3.183  5.490   0.70 13.11 ?  125 PRO   A HD3  1 
ATOM   2599 H  HD3  B PRO   A 1 125 ? 20.598 -3.109  5.584   0.30 13.37 ?  125 PRO   A HD3  1 
ATOM   2600 N  N    A LEU   A 1 126 ? 16.938 -5.242  2.333   0.70 10.88 ?  126 LEU   A N    1 
ATOM   2601 N  N    B LEU   A 1 126 ? 16.855 -4.892  2.356   0.30 10.85 ?  126 LEU   A N    1 
ATOM   2602 C  CA   A LEU   A 1 126 ? 16.947 -6.064  1.132   0.70 11.51 ?  126 LEU   A CA   1 
ATOM   2603 C  CA   B LEU   A 1 126 ? 16.851 -5.721  1.157   0.30 10.46 ?  126 LEU   A CA   1 
ATOM   2604 C  C    A LEU   A 1 126 ? 17.875 -5.449  0.089   0.70 11.69 ?  126 LEU   A C    1 
ATOM   2605 C  C    B LEU   A 1 126 ? 17.810 -5.128  0.130   0.30 10.43 ?  126 LEU   A C    1 
ATOM   2606 O  O    A LEU   A 1 126 ? 17.643 -4.335  -0.391  0.70 12.41 ?  126 LEU   A O    1 
ATOM   2607 O  O    B LEU   A 1 126 ? 17.590 -4.018  -0.364  0.30 11.05 ?  126 LEU   A O    1 
ATOM   2608 C  CB   A LEU   A 1 126 ? 15.535 -6.215  0.583   0.70 11.67 ?  126 LEU   A CB   1 
ATOM   2609 C  CB   B LEU   A 1 126 ? 15.445 -5.808  0.576   0.30 11.22 ?  126 LEU   A CB   1 
ATOM   2610 C  CG   A LEU   A 1 126 ? 14.641 -7.176  1.364   0.70 12.39 ?  126 LEU   A CG   1 
ATOM   2611 C  CG   B LEU   A 1 126 ? 14.436 -6.664  1.342   0.30 11.33 ?  126 LEU   A CG   1 
ATOM   2612 C  CD1  A LEU   A 1 126 ? 13.211 -7.036  0.892   0.70 13.85 ?  126 LEU   A CD1  1 
ATOM   2613 C  CD1  B LEU   A 1 126 ? 13.055 -6.513  0.729   0.30 11.86 ?  126 LEU   A CD1  1 
ATOM   2614 C  CD2  A LEU   A 1 126 ? 15.119 -8.615  1.200   0.70 12.28 ?  126 LEU   A CD2  1 
ATOM   2615 C  CD2  B LEU   A 1 126 ? 14.848 -8.127  1.352   0.30 11.32 ?  126 LEU   A CD2  1 
ATOM   2616 H  H    A LEU   A 1 126 ? 16.219 -4.782  2.443   0.70 13.04 ?  126 LEU   A H    1 
ATOM   2617 H  H    B LEU   A 1 126 ? 16.179 -4.361  2.433   0.30 13.00 ?  126 LEU   A H    1 
ATOM   2618 H  HA   A LEU   A 1 126 ? 17.283 -6.944  1.348   0.70 13.80 ?  126 LEU   A HA   1 
ATOM   2619 H  HA   B LEU   A 1 126 ? 17.156 -6.612  1.387   0.30 12.54 ?  126 LEU   A HA   1 
ATOM   2620 H  HB2  A LEU   A 1 126 ? 15.099 -5.346  0.595   0.70 13.99 ?  126 LEU   A HB2  1 
ATOM   2621 H  HB2  B LEU   A 1 126 ? 15.083 -4.910  0.528   0.30 13.45 ?  126 LEU   A HB2  1 
ATOM   2622 H  HB3  A LEU   A 1 126 ? 15.582 -6.541  -0.328  0.70 13.99 ?  126 LEU   A HB3  1 
ATOM   2623 H  HB3  B LEU   A 1 126 ? 15.515 -6.176  -0.316  0.30 13.45 ?  126 LEU   A HB3  1 
ATOM   2624 H  HG   A LEU   A 1 126 ? 14.671 -6.955  2.309   0.70 14.85 ?  126 LEU   A HG   1 
ATOM   2625 H  HG   B LEU   A 1 126 ? 14.390 -6.357  2.261   0.30 13.58 ?  126 LEU   A HG   1 
ATOM   2626 H  HD11 A LEU   A 1 126 ? 12.650 -7.655  1.386   0.70 16.60 ?  126 LEU   A HD11 1 
ATOM   2627 H  HD11 B LEU   A 1 126 ? 12.421 -7.035  1.246   0.30 14.22 ?  126 LEU   A HD11 1 
ATOM   2628 H  HD12 A LEU   A 1 126 ? 12.916 -6.125  1.049   0.70 16.60 ?  126 LEU   A HD12 1 
ATOM   2629 H  HD12 B LEU   A 1 126 ? 12.802 -5.578  0.740   0.30 14.22 ?  126 LEU   A HD12 1 
ATOM   2630 H  HD13 A LEU   A 1 126 ? 13.170 -7.238  -0.056  0.70 16.60 ?  126 LEU   A HD13 1 
ATOM   2631 H  HD13 B LEU   A 1 126 ? 13.079 -6.837  -0.186  0.30 14.22 ?  126 LEU   A HD13 1 
ATOM   2632 H  HD21 A LEU   A 1 126 ? 14.456 -9.217  1.570   0.70 14.72 ?  126 LEU   A HD21 1 
ATOM   2633 H  HD21 B LEU   A 1 126 ? 14.129 -8.653  1.734   0.30 13.56 ?  126 LEU   A HD21 1 
ATOM   2634 H  HD22 A LEU   A 1 126 ? 15.242 -8.800  0.254   0.70 14.72 ?  126 LEU   A HD22 1 
ATOM   2635 H  HD22 B LEU   A 1 126 ? 15.017 -8.411  0.440   0.30 13.56 ?  126 LEU   A HD22 1 
ATOM   2636 H  HD23 A LEU   A 1 126 ? 15.963 -8.724  1.668   0.70 14.72 ?  126 LEU   A HD23 1 
ATOM   2637 H  HD23 B LEU   A 1 126 ? 15.651 -8.225  1.884   0.30 13.56 ?  126 LEU   A HD23 1 
ATOM   2638 N  N    A LEU   A 1 127 ? 18.924 -6.184  -0.264  0.70 11.53 ?  127 LEU   A N    1 
ATOM   2639 N  N    B LEU   A 1 127 ? 18.868 -5.863  -0.198  0.30 10.32 ?  127 LEU   A N    1 
ATOM   2640 C  CA   A LEU   A 1 127 ? 19.913 -5.682  -1.203  0.70 11.25 ?  127 LEU   A CA   1 
ATOM   2641 C  CA   B LEU   A 1 127 ? 19.864 -5.347  -1.125  0.30 10.52 ?  127 LEU   A CA   1 
ATOM   2642 C  C    A LEU   A 1 127 ? 19.298 -5.494  -2.581  0.70 10.70 ?  127 LEU   A C    1 
ATOM   2643 C  C    B LEU   A 1 127 ? 19.301 -5.263  -2.539  0.30 10.79 ?  127 LEU   A C    1 
ATOM   2644 O  O    A LEU   A 1 127 ? 18.457 -6.284  -3.028  0.70 10.89 ?  127 LEU   A O    1 
ATOM   2645 O  O    B LEU   A 1 127 ? 18.483 -6.084  -2.965  0.30 11.22 ?  127 LEU   A O    1 
ATOM   2646 C  CB   A LEU   A 1 127 ? 21.089 -6.652  -1.294  0.70 11.59 ?  127 LEU   A CB   1 
ATOM   2647 C  CB   B LEU   A 1 127 ? 21.108 -6.235  -1.128  0.30 10.74 ?  127 LEU   A CB   1 
ATOM   2648 C  CG   A LEU   A 1 127 ? 21.887 -6.880  -0.011  0.70 11.92 ?  127 LEU   A CG   1 
ATOM   2649 C  CG   B LEU   A 1 127 ? 21.909 -6.278  0.178   0.30 11.15 ?  127 LEU   A CG   1 
ATOM   2650 C  CD1  A LEU   A 1 127 ? 22.981 -7.878  -0.282  0.70 12.26 ?  127 LEU   A CD1  1 
ATOM   2651 C  CD1  B LEU   A 1 127 ? 23.061 -7.264  0.067   0.30 11.48 ?  127 LEU   A CD1  1 
ATOM   2652 C  CD2  A LEU   A 1 127 ? 22.484 -5.589  0.497   0.70 12.71 ?  127 LEU   A CD2  1 
ATOM   2653 C  CD2  B LEU   A 1 127 ? 22.422 -4.889  0.558   0.30 11.68 ?  127 LEU   A CD2  1 
ATOM   2654 H  H    A LEU   A 1 127 ? 19.082 -6.974  0.034   0.70 13.82 ?  127 LEU   A H    1 
ATOM   2655 H  H    B LEU   A 1 127 ? 19.033 -6.652  0.102   0.30 12.37 ?  127 LEU   A H    1 
ATOM   2656 H  HA   A LEU   A 1 127 ? 20.248 -4.827  -0.893  0.70 13.48 ?  127 LEU   A HA   1 
ATOM   2657 H  HA   B LEU   A 1 127 ? 20.123 -4.454  -0.842  0.30 12.60 ?  127 LEU   A HA   1 
ATOM   2658 H  HB2  A LEU   A 1 127 ? 20.747 -7.515  -1.577  0.70 13.89 ?  127 LEU   A HB2  1 
ATOM   2659 H  HB2  B LEU   A 1 127 ? 20.830 -7.141  -1.334  0.30 12.87 ?  127 LEU   A HB2  1 
ATOM   2660 H  HB3  A LEU   A 1 127 ? 21.707 -6.317  -1.960  0.70 13.89 ?  127 LEU   A HB3  1 
ATOM   2661 H  HB3  B LEU   A 1 127 ? 21.702 -5.915  -1.827  0.30 12.87 ?  127 LEU   A HB3  1 
ATOM   2662 H  HG   A LEU   A 1 127 ? 21.302 -7.244  0.676   0.70 14.29 ?  127 LEU   A HG   1 
ATOM   2663 H  HG   B LEU   A 1 127 ? 21.326 -6.583  0.889   0.30 13.36 ?  127 LEU   A HG   1 
ATOM   2664 H  HD11 A LEU   A 1 127 ? 23.465 -8.048  0.541   0.70 14.70 ?  127 LEU   A HD11 1 
ATOM   2665 H  HD11 B LEU   A 1 127 ? 23.576 -7.237  0.888   0.30 13.76 ?  127 LEU   A HD11 1 
ATOM   2666 H  HD12 A LEU   A 1 127 ? 22.585 -8.703  -0.608  0.70 14.70 ?  127 LEU   A HD12 1 
ATOM   2667 H  HD12 B LEU   A 1 127 ? 22.701 -8.155  -0.068  0.30 13.76 ?  127 LEU   A HD12 1 
ATOM   2668 H  HD13 A LEU   A 1 127 ? 23.581 -7.514  -0.950  0.70 14.70 ?  127 LEU   A HD13 1 
ATOM   2669 H  HD13 B LEU   A 1 127 ? 23.620 -7.014  -0.684  0.30 13.76 ?  127 LEU   A HD13 1 
ATOM   2670 H  HD21 A LEU   A 1 127 ? 23.084 -5.786  1.232   0.70 15.23 ?  127 LEU   A HD21 1 
ATOM   2671 H  HD21 B LEU   A 1 127 ? 23.033 -4.976  1.308   0.30 13.99 ?  127 LEU   A HD21 1 
ATOM   2672 H  HD22 A LEU   A 1 127 ? 22.980 -5.168  -0.228  0.70 15.23 ?  127 LEU   A HD22 1 
ATOM   2673 H  HD22 B LEU   A 1 127 ? 22.885 -4.504  -0.202  0.30 13.99 ?  127 LEU   A HD22 1 
ATOM   2674 H  HD23 A LEU   A 1 127 ? 21.774 -5.003  0.793   0.70 15.23 ?  127 LEU   A HD23 1 
ATOM   2675 H  HD23 B LEU   A 1 127 ? 21.670 -4.331  0.808   0.30 13.99 ?  127 LEU   A HD23 1 
ATOM   2676 N  N    A SER   A 1 128 ? 19.737 -4.440  -3.257  0.70 10.97 ?  128 SER   A N    1 
ATOM   2677 N  N    B SER   A 1 128 ? 19.746 -4.235  -3.259  0.30 11.03 ?  128 SER   A N    1 
ATOM   2678 C  CA   A SER   A 1 128 ? 19.321 -4.048  -4.595  0.70 11.47 ?  128 SER   A CA   1 
ATOM   2679 C  CA   B SER   A 1 128 ? 19.424 -4.017  -4.666  0.30 10.87 ?  128 SER   A CA   1 
ATOM   2680 C  C    A SER   A 1 128 ? 17.858 -3.608  -4.678  0.70 11.95 ?  128 SER   A C    1 
ATOM   2681 C  C    B SER   A 1 128 ? 17.993 -3.544  -4.899  0.30 10.87 ?  128 SER   A C    1 
ATOM   2682 O  O    A SER   A 1 128 ? 17.393 -3.298  -5.775  0.70 13.00 ?  128 SER   A O    1 
ATOM   2683 O  O    B SER   A 1 128 ? 17.644 -3.189  -6.028  0.30 10.98 ?  128 SER   A O    1 
ATOM   2684 C  CB   A SER   A 1 128 ? 19.656 -5.095  -5.669  0.70 11.93 ?  128 SER   A CB   1 
ATOM   2685 C  CB   B SER   A 1 128 ? 19.752 -5.243  -5.520  0.30 10.76 ?  128 SER   A CB   1 
ATOM   2686 O  OG   A SER   A 1 128 ? 21.057 -5.337  -5.713  0.70 12.51 ?  128 SER   A OG   1 
ATOM   2687 O  OG   B SER   A 1 128 ? 21.152 -5.342  -5.723  0.30 11.25 ?  128 SER   A OG   1 
ATOM   2688 H  H    A SER   A 1 128 ? 20.337 -3.905  -2.935  0.70 13.15 ?  128 SER   A H    1 
ATOM   2689 H  H    B SER   A 1 128 ? 20.262 -3.624  -2.939  0.30 13.22 ?  128 SER   A H    1 
ATOM   2690 H  HA   A SER   A 1 128 ? 19.843 -3.267  -4.823  0.70 13.75 ?  128 SER   A HA   1 
ATOM   2691 H  HA   B SER   A 1 128 ? 19.992 -3.303  -4.979  0.30 13.03 ?  128 SER   A HA   1 
ATOM   2692 H  HB2  A SER   A 1 128 ? 19.195 -5.921  -5.464  0.70 14.30 ?  128 SER   A HB2  1 
ATOM   2693 H  HB2  B SER   A 1 128 ? 19.426 -6.041  -5.080  0.30 12.90 ?  128 SER   A HB2  1 
ATOM   2694 H  HB3  A SER   A 1 128 ? 19.367 -4.758  -6.535  0.70 14.30 ?  128 SER   A HB3  1 
ATOM   2695 H  HB3  B SER   A 1 128 ? 19.323 -5.141  -6.386  0.30 12.90 ?  128 SER   A HB3  1 
ATOM   2696 H  HG   A SER   A 1 128 ? 21.465 -4.624  -5.888  0.70 15.00 ?  128 SER   A HG   1 
ATOM   2697 H  HG   B SER   A 1 128 ? 21.432 -4.627  -6.071  0.30 13.49 ?  128 SER   A HG   1 
ATOM   2698 N  N    A ALA   A 1 129 ? 17.129 -3.554  -3.561  0.70 12.35 ?  129 ALA   A N    1 
ATOM   2699 N  N    B ALA   A 1 129 ? 17.171 -3.508  -3.852  0.30 11.34 ?  129 ALA   A N    1 
ATOM   2700 C  CA   A ALA   A 1 129 ? 15.752 -3.071  -3.550  0.70 12.29 ?  129 ALA   A CA   1 
ATOM   2701 C  CA   B ALA   A 1 129 ? 15.817 -2.993  -3.968  0.30 11.80 ?  129 ALA   A CA   1 
ATOM   2702 C  C    A ALA   A 1 129 ? 15.745 -1.539  -3.535  0.70 11.93 ?  129 ALA   A C    1 
ATOM   2703 C  C    B ALA   A 1 129 ? 15.813 -1.476  -3.765  0.30 12.31 ?  129 ALA   A C    1 
ATOM   2704 O  O    A ALA   A 1 129 ? 16.784 -0.882  -3.668  0.70 12.42 ?  129 ALA   A O    1 
ATOM   2705 O  O    B ALA   A 1 129 ? 16.850 -0.848  -3.533  0.30 12.28 ?  129 ALA   A O    1 
ATOM   2706 C  CB   A ALA   A 1 129 ? 14.982 -3.680  -2.376  0.70 13.44 ?  129 ALA   A CB   1 
ATOM   2707 C  CB   B ALA   A 1 129 ? 14.882 -3.710  -2.995  0.30 12.37 ?  129 ALA   A CB   1 
ATOM   2708 H  H    A ALA   A 1 129 ? 17.415 -3.797  -2.785  0.70 14.80 ?  129 ALA   A H    1 
ATOM   2709 H  H    B ALA   A 1 129 ? 17.375 -3.774  -3.059  0.30 13.59 ?  129 ALA   A H    1 
ATOM   2710 H  HA   A ALA   A 1 129 ? 15.317 -3.359  -4.365  0.70 14.73 ?  129 ALA   A HA   1 
ATOM   2711 H  HA   B ALA   A 1 129 ? 15.498 -3.164  -4.862  0.30 14.15 ?  129 ALA   A HA   1 
ATOM   2712 H  HB1  A ALA   A 1 129 ? 14.069 -3.350  -2.393  0.70 16.11 ?  129 ALA   A HB1  1 
ATOM   2713 H  HB1  B ALA   A 1 129 ? 13.995 -3.323  -3.068  0.30 14.83 ?  129 ALA   A HB1  1 
ATOM   2714 H  HB2  A ALA   A 1 129 ? 14.988 -4.644  -2.460  0.70 16.11 ?  129 ALA   A HB2  1 
ATOM   2715 H  HB2  B ALA   A 1 129 ? 14.854 -4.650  -3.226  0.30 14.83 ?  129 ALA   A HB2  1 
ATOM   2716 H  HB3  A ALA   A 1 129 ? 15.412 -3.417  -1.546  0.70 16.11 ?  129 ALA   A HB3  1 
ATOM   2717 H  HB3  B ALA   A 1 129 ? 15.217 -3.599  -2.092  0.30 14.83 ?  129 ALA   A HB3  1 
ATOM   2718 N  N    A GLY   A 1 130 ? 14.556 -0.956  -3.392  0.70 11.51 ?  130 GLY   A N    1 
ATOM   2719 N  N    B GLY   A 1 130 ? 14.630 -0.879  -3.864  0.30 12.85 ?  130 GLY   A N    1 
ATOM   2720 C  CA   A GLY   A 1 130 ? 14.447 0.493   -3.354  0.70 12.23 ?  130 GLY   A CA   1 
ATOM   2721 C  CA   B GLY   A 1 130 ? 14.532 0.567   -3.747  0.30 13.37 ?  130 GLY   A CA   1 
ATOM   2722 C  C    A GLY   A 1 130 ? 15.049 1.122   -4.591  0.70 11.72 ?  130 GLY   A C    1 
ATOM   2723 C  C    B GLY   A 1 130 ? 15.249 1.246   -4.894  0.30 13.43 ?  130 GLY   A C    1 
ATOM   2724 O  O    A GLY   A 1 130 ? 14.812 0.674   -5.717  0.70 11.71 ?  130 GLY   A O    1 
ATOM   2725 O  O    B GLY   A 1 130 ? 15.097 0.870   -6.062  0.30 14.00 ?  130 GLY   A O    1 
ATOM   2726 H  H    A GLY   A 1 130 ? 13.804 -1.371  -3.325  0.70 13.80 ?  130 GLY   A H    1 
ATOM   2727 H  H    B GLY   A 1 130 ? 13.883 -1.281  -4.002  0.30 15.41 ?  130 GLY   A H    1 
ATOM   2728 H  HA2  A GLY   A 1 130 ? 13.509 0.748   -3.305  0.70 14.67 ?  130 GLY   A HA2  1 
ATOM   2729 H  HA2  B GLY   A 1 130 ? 13.594 0.839   -3.728  0.30 16.03 ?  130 GLY   A HA2  1 
ATOM   2730 H  HA3  A GLY   A 1 130 ? 14.906 0.837   -2.584  0.70 14.67 ?  130 GLY   A HA3  1 
ATOM   2731 H  HA3  B GLY   A 1 130 ? 14.955 0.867   -2.933  0.30 16.03 ?  130 GLY   A HA3  1 
ATOM   2732 N  N    A ILE   A 1 131 ? 15.836 2.185   -4.385  0.70 12.50 ?  131 ILE   A N    1 
ATOM   2733 N  N    B ILE   A 1 131 ? 16.072 2.245   -4.558  0.30 13.06 ?  131 ILE   A N    1 
ATOM   2734 C  CA   A ILE   A 1 131 ? 16.388 2.957   -5.497  0.70 12.74 ?  131 ILE   A CA   1 
ATOM   2735 C  CA   B ILE   A 1 131 ? 16.702 3.067   -5.586  0.30 12.94 ?  131 ILE   A CA   1 
ATOM   2736 C  C    A ILE   A 1 131 ? 17.430 2.199   -6.309  0.70 12.60 ?  131 ILE   A C    1 
ATOM   2737 C  C    B ILE   A 1 131 ? 17.659 2.268   -6.455  0.30 12.69 ?  131 ILE   A C    1 
ATOM   2738 O  O    A ILE   A 1 131 ? 17.860 2.710   -7.351  0.70 13.64 ?  131 ILE   A O    1 
ATOM   2739 O  O    B ILE   A 1 131 ? 18.037 2.733   -7.537  0.30 13.10 ?  131 ILE   A O    1 
ATOM   2740 C  CB   A ILE   A 1 131 ? 16.918 4.338   -5.050  0.70 13.69 ?  131 ILE   A CB   1 
ATOM   2741 C  CB   B ILE   A 1 131 ? 17.384 4.321   -4.992  0.30 13.39 ?  131 ILE   A CB   1 
ATOM   2742 C  CG1  A ILE   A 1 131 ? 18.155 4.199   -4.155  0.70 14.99 ?  131 ILE   A CG1  1 
ATOM   2743 C  CG1  B ILE   A 1 131 ? 18.594 3.947   -4.130  0.30 13.95 ?  131 ILE   A CG1  1 
ATOM   2744 C  CG2  A ILE   A 1 131 ? 15.819 5.134   -4.347  0.70 14.16 ?  131 ILE   A CG2  1 
ATOM   2745 C  CG2  B ILE   A 1 131 ? 16.386 5.143   -4.190  0.30 13.48 ?  131 ILE   A CG2  1 
ATOM   2746 C  CD1  A ILE   A 1 131 ? 18.799 5.531   -3.789  0.70 16.18 ?  131 ILE   A CD1  1 
ATOM   2747 C  CD1  B ILE   A 1 131 ? 19.317 5.154   -3.537  0.30 14.02 ?  131 ILE   A CD1  1 
ATOM   2748 H  H    A ILE   A 1 131 ? 16.044 2.490   -3.607  0.70 14.98 ?  131 ILE   A H    1 
ATOM   2749 H  H    B ILE   A 1 131 ? 16.279 2.459   -3.750  0.30 15.65 ?  131 ILE   A H    1 
ATOM   2750 H  HA   A ILE   A 1 131 ? 15.664 3.141   -6.110  0.70 15.27 ?  131 ILE   A HA   1 
ATOM   2751 H  HA   B ILE   A 1 131 ? 16.005 3.384   -6.170  0.30 15.51 ?  131 ILE   A HA   1 
ATOM   2752 H  HB   A ILE   A 1 131 ? 17.179 4.832   -5.840  0.70 16.41 ?  131 ILE   A HB   1 
ATOM   2753 H  HB   B ILE   A 1 131 ? 17.695 4.866   -5.730  0.30 16.06 ?  131 ILE   A HB   1 
ATOM   2754 H  HG12 A ILE   A 1 131 ? 17.902 3.756   -3.331  0.70 17.97 ?  131 ILE   A HG12 1 
ATOM   2755 H  HG12 B ILE   A 1 131 ? 18.298 3.391   -3.395  0.30 16.73 ?  131 ILE   A HG12 1 
ATOM   2756 H  HG13 A ILE   A 1 131 ? 18.826 3.671   -4.618  0.70 17.97 ?  131 ILE   A HG13 1 
ATOM   2757 H  HG13 B ILE   A 1 131 ? 19.235 3.466   -4.675  0.30 16.73 ?  131 ILE   A HG13 1 
ATOM   2758 H  HG21 A ILE   A 1 131 ? 16.122 6.043   -4.209  0.70 16.98 ?  131 ILE   A HG21 1 
ATOM   2759 H  HG21 B ILE   A 1 131 ? 16.772 6.012   -4.002  0.30 16.16 ?  131 ILE   A HG21 1 
ATOM   2760 H  HG22 A ILE   A 1 131 ? 15.025 5.128   -4.904  0.70 16.98 ?  131 ILE   A HG22 1 
ATOM   2761 H  HG22 B ILE   A 1 131 ? 15.576 5.247   -4.712  0.30 16.16 ?  131 ILE   A HG22 1 
ATOM   2762 H  HG23 A ILE   A 1 131 ? 15.624 4.715   -3.492  0.70 16.98 ?  131 ILE   A HG23 1 
ATOM   2763 H  HG23 B ILE   A 1 131 ? 16.189 4.678   -3.362  0.30 16.16 ?  131 ILE   A HG23 1 
ATOM   2764 H  HD11 A ILE   A 1 131 ? 19.634 5.361   -3.321  0.70 19.40 ?  131 ILE   A HD11 1 
ATOM   2765 H  HD11 B ILE   A 1 131 ? 20.148 4.859   -3.131  0.30 16.81 ?  131 ILE   A HD11 1 
ATOM   2766 H  HD12 A ILE   A 1 131 ? 18.974 6.032   -4.601  0.70 19.40 ?  131 ILE   A HD12 1 
ATOM   2767 H  HD12 B ILE   A 1 131 ? 19.505 5.792   -4.245  0.30 16.81 ?  131 ILE   A HD12 1 
ATOM   2768 H  HD13 A ILE   A 1 131 ? 18.196 6.028   -3.215  0.70 19.40 ?  131 ILE   A HD13 1 
ATOM   2769 H  HD13 B ILE   A 1 131 ? 18.751 5.568   -2.865  0.30 16.81 ?  131 ILE   A HD13 1 
ATOM   2770 N  N    A PHE   A 1 132 ? 17.844 0.995   -5.878  0.70 12.64 ?  132 PHE   A N    1 
ATOM   2771 N  N    B PHE   A 1 132 ? 18.065 1.071   -6.015  0.30 12.58 ?  132 PHE   A N    1 
ATOM   2772 C  CA   A PHE   A 1 132 ? 18.718 0.162   -6.699  0.70 12.76 ?  132 PHE   A CA   1 
ATOM   2773 C  CA   B PHE   A 1 132 ? 18.971 0.259   -6.818  0.30 12.76 ?  132 PHE   A CA   1 
ATOM   2774 C  C    A PHE   A 1 132 ? 17.956 -0.604  -7.784  0.70 12.81 ?  132 PHE   A C    1 
ATOM   2775 C  C    B PHE   A 1 132 ? 18.269 -0.457  -7.973  0.30 13.60 ?  132 PHE   A C    1 
ATOM   2776 O  O    A PHE   A 1 132 ? 18.589 -1.252  -8.627  0.70 13.23 ?  132 PHE   A O    1 
ATOM   2777 O  O    B PHE   A 1 132 ? 18.950 -0.937  -8.886  0.30 14.10 ?  132 PHE   A O    1 
ATOM   2778 C  CB   A PHE   A 1 132 ? 19.526 -0.813  -5.829  0.70 12.40 ?  132 PHE   A CB   1 
ATOM   2779 C  CB   B PHE   A 1 132 ? 19.735 -0.730  -5.933  0.30 11.91 ?  132 PHE   A CB   1 
ATOM   2780 C  CG   A PHE   A 1 132 ? 20.770 -0.214  -5.189  0.70 12.17 ?  132 PHE   A CG   1 
ATOM   2781 C  CG   B PHE   A 1 132 ? 20.889 -0.113  -5.178  0.30 11.60 ?  132 PHE   A CG   1 
ATOM   2782 C  CD1  A PHE   A 1 132 ? 20.688 0.853   -4.309  0.70 12.74 ?  132 PHE   A CD1  1 
ATOM   2783 C  CD1  B PHE   A 1 132 ? 20.666 0.762   -4.125  0.30 12.06 ?  132 PHE   A CD1  1 
ATOM   2784 C  CD2  A PHE   A 1 132 ? 22.016 -0.776  -5.428  0.70 12.53 ?  132 PHE   A CD2  1 
ATOM   2785 C  CD2  B PHE   A 1 132 ? 22.196 -0.428  -5.510  0.30 11.74 ?  132 PHE   A CD2  1 
ATOM   2786 C  CE1  A PHE   A 1 132 ? 21.835 1.369   -3.710  0.70 12.97 ?  132 PHE   A CE1  1 
ATOM   2787 C  CE1  B PHE   A 1 132 ? 21.729 1.318   -3.428  0.30 12.12 ?  132 PHE   A CE1  1 
ATOM   2788 C  CE2  A PHE   A 1 132 ? 23.161 -0.268  -4.833  0.70 12.72 ?  132 PHE   A CE2  1 
ATOM   2789 C  CE2  B PHE   A 1 132 ? 23.261 0.125   -4.818  0.30 11.86 ?  132 PHE   A CE2  1 
ATOM   2790 C  CZ   A PHE   A 1 132 ? 23.067 0.807   -3.972  0.70 12.96 ?  132 PHE   A CZ   1 
ATOM   2791 C  CZ   B PHE   A 1 132 ? 23.024 0.999   -3.776  0.30 11.91 ?  132 PHE   A CZ   1 
ATOM   2792 H  H    A PHE   A 1 132 ? 17.629 0.646   -5.118  0.70 15.16 ?  132 PHE   A H    1 
ATOM   2793 H  H    B PHE   A 1 132 ? 17.840 0.719   -5.256  0.30 15.08 ?  132 PHE   A H    1 
ATOM   2794 H  HA   A PHE   A 1 132 ? 19.356 0.742   -7.139  0.70 15.29 ?  132 PHE   A HA   1 
ATOM   2795 H  HA   B PHE   A 1 132 ? 19.630 0.857   -7.198  0.30 15.29 ?  132 PHE   A HA   1 
ATOM   2796 H  HB2  A PHE   A 1 132 ? 18.958 -1.136  -5.111  0.70 14.87 ?  132 PHE   A HB2  1 
ATOM   2797 H  HB2  B PHE   A 1 132 ? 19.125 -1.103  -5.281  0.30 14.28 ?  132 PHE   A HB2  1 
ATOM   2798 H  HB3  A PHE   A 1 132 ? 19.810 -1.559  -6.380  0.70 14.87 ?  132 PHE   A HB3  1 
ATOM   2799 H  HB3  B PHE   A 1 132 ? 20.094 -1.434  -6.494  0.30 14.28 ?  132 PHE   A HB3  1 
ATOM   2800 H  HD1  A PHE   A 1 132 ? 19.864 1.235   -4.121  0.70 15.28 ?  132 PHE   A HD1  1 
ATOM   2801 H  HD1  B PHE   A 1 132 ? 19.796 0.983   -3.884  0.30 14.46 ?  132 PHE   A HD1  1 
ATOM   2802 H  HD2  A PHE   A 1 132 ? 22.091 -1.502  -6.006  0.70 15.02 ?  132 PHE   A HD2  1 
ATOM   2803 H  HD2  B PHE   A 1 132 ? 22.362 -1.015  -6.212  0.30 14.07 ?  132 PHE   A HD2  1 
ATOM   2804 H  HE1  A PHE   A 1 132 ? 21.773 2.093   -3.126  0.70 15.54 ?  132 PHE   A HE1  1 
ATOM   2805 H  HE1  B PHE   A 1 132 ? 21.568 1.908   -2.726  0.30 14.53 ?  132 PHE   A HE1  1 
ATOM   2806 H  HE2  A PHE   A 1 132 ? 23.993 -0.648  -5.014  0.70 15.24 ?  132 PHE   A HE2  1 
ATOM   2807 H  HE2  B PHE   A 1 132 ? 24.134 -0.092  -5.056  0.30 14.22 ?  132 PHE   A HE2  1 
ATOM   2808 H  HZ   A PHE   A 1 132 ? 23.835 1.156   -3.571  0.70 15.54 ?  132 PHE   A HZ   1 
ATOM   2809 H  HZ   B PHE   A 1 132 ? 23.737 1.372   -3.310  0.30 14.28 ?  132 PHE   A HZ   1 
ATOM   2810 N  N    A GLY   A 1 133 ? 16.621 -0.561  -7.780  0.70 12.78 ?  133 GLY   A N    1 
ATOM   2811 N  N    B GLY   A 1 133 ? 16.937 -0.555  -7.954  0.30 13.70 ?  133 GLY   A N    1 
ATOM   2812 C  CA   A GLY   A 1 133 ? 15.830 -0.926  -8.940  0.70 13.75 ?  133 GLY   A CA   1 
ATOM   2813 C  CA   B GLY   A 1 133 ? 16.161 -0.899  -9.131  0.30 13.86 ?  133 GLY   A CA   1 
ATOM   2814 C  C    A GLY   A 1 133 ? 15.552 -2.400  -9.169  0.70 14.38 ?  133 GLY   A C    1 
ATOM   2815 C  C    B GLY   A 1 133 ? 15.525 -2.277  -9.133  0.30 14.00 ?  133 GLY   A C    1 
ATOM   2816 O  O    A GLY   A 1 133 ? 14.967 -2.732  -10.207 0.70 15.17 ?  133 GLY   A O    1 
ATOM   2817 O  O    B GLY   A 1 133 ? 14.610 -2.510  -9.933  0.30 14.04 ?  133 GLY   A O    1 
ATOM   2818 H  H    A GLY   A 1 133 ? 16.148 -0.320  -7.104  0.70 15.31 ?  133 GLY   A H    1 
ATOM   2819 H  H    B GLY   A 1 133 ? 16.459 -0.428  -7.250  0.30 16.42 ?  133 GLY   A H    1 
ATOM   2820 H  HA2  A GLY   A 1 133 ? 14.971 -0.483  -8.873  0.70 16.48 ?  133 GLY   A HA2  1 
ATOM   2821 H  HA2  B GLY   A 1 133 ? 15.445 -0.257  -9.235  0.30 16.62 ?  133 GLY   A HA2  1 
ATOM   2822 H  HA3  A GLY   A 1 133 ? 16.274 -0.588  -9.732  0.70 16.48 ?  133 GLY   A HA3  1 
ATOM   2823 H  HA3  B GLY   A 1 133 ? 16.732 -0.828  -9.914  0.30 16.62 ?  133 GLY   A HA3  1 
ATOM   2824 N  N    A ALA   A 1 134 ? 15.953 -3.294  -8.269  0.70 13.98 ?  134 ALA   A N    1 
ATOM   2825 N  N    B ALA   A 1 134 ? 15.967 -3.193  -8.276  0.30 13.98 ?  134 ALA   A N    1 
ATOM   2826 C  CA   A ALA   A 1 134 ? 15.633 -4.702  -8.448  0.70 14.68 ?  134 ALA   A CA   1 
ATOM   2827 C  CA   B ALA   A 1 134 ? 15.527 -4.577  -8.369  0.30 13.96 ?  134 ALA   A CA   1 
ATOM   2828 C  C    A ALA   A 1 134 ? 14.270 -5.019  -7.836  0.70 14.65 ?  134 ALA   A C    1 
ATOM   2829 C  C    B ALA   A 1 134 ? 14.216 -4.805  -7.620  0.30 13.63 ?  134 ALA   A C    1 
ATOM   2830 O  O    A ALA   A 1 134 ? 13.689 -4.228  -7.089  0.70 15.51 ?  134 ALA   A O    1 
ATOM   2831 O  O    B ALA   A 1 134 ? 13.815 -4.023  -6.754  0.30 13.84 ?  134 ALA   A O    1 
ATOM   2832 C  CB   A ALA   A 1 134 ? 16.719 -5.594  -7.848  0.70 15.72 ?  134 ALA   A CB   1 
ATOM   2833 C  CB   B ALA   A 1 134 ? 16.590 -5.527  -7.822  0.30 14.51 ?  134 ALA   A CB   1 
ATOM   2834 H  H    A ALA   A 1 134 ? 16.410 -3.109  -7.560  0.70 16.76 ?  134 ALA   A H    1 
ATOM   2835 H  H    B ALA   A 1 134 ? 16.517 -3.032  -7.635  0.30 16.76 ?  134 ALA   A H    1 
ATOM   2836 H  HA   A ALA   A 1 134 ? 15.584 -4.891  -9.399  0.70 17.61 ?  134 ALA   A HA   1 
ATOM   2837 H  HA   B ALA   A 1 134 ? 15.381 -4.791  -9.303  0.30 16.74 ?  134 ALA   A HA   1 
ATOM   2838 H  HB1  A ALA   A 1 134 ? 16.485 -6.519  -8.005  0.70 18.84 ?  134 ALA   A HB1  1 
ATOM   2839 H  HB1  B ALA   A 1 134 ? 16.267 -6.436  -7.910  0.30 17.40 ?  134 ALA   A HB1  1 
ATOM   2840 H  HB2  A ALA   A 1 134 ? 17.567 -5.388  -8.277  0.70 18.84 ?  134 ALA   A HB2  1 
ATOM   2841 H  HB2  B ALA   A 1 134 ? 17.404 -5.409  -8.332  0.30 17.40 ?  134 ALA   A HB2  1 
ATOM   2842 H  HB3  A ALA   A 1 134 ? 16.780 -5.419  -6.897  0.70 18.84 ?  134 ALA   A HB3  1 
ATOM   2843 H  HB3  B ALA   A 1 134 ? 16.746 -5.317  -6.889  0.30 17.40 ?  134 ALA   A HB3  1 
ATOM   2844 N  N    A ASP   A 1 135 ? 13.761 -6.198  -8.171  0.70 14.75 ?  135 ASP   A N    1 
ATOM   2845 N  N    B ASP   A 1 135 ? 13.562 -5.912  -7.962  0.30 13.98 ?  135 ASP   A N    1 
ATOM   2846 C  CA   A ASP   A 1 135 ? 12.498 -6.679  -7.620  0.70 15.47 ?  135 ASP   A CA   1 
ATOM   2847 C  CA   B ASP   A 1 135 ? 12.306 -6.300  -7.332  0.30 14.32 ?  135 ASP   A CA   1 
ATOM   2848 C  C    A ASP   A 1 135 ? 12.721 -7.119  -6.180  0.70 14.76 ?  135 ASP   A C    1 
ATOM   2849 C  C    B ASP   A 1 135 ? 12.578 -6.785  -5.914  0.30 13.56 ?  135 ASP   A C    1 
ATOM   2850 O  O    A ASP   A 1 135 ? 13.517 -8.036  -5.944  0.70 14.63 ?  135 ASP   A O    1 
ATOM   2851 O  O    B ASP   A 1 135 ? 13.309 -7.769  -5.735  0.30 13.28 ?  135 ASP   A O    1 
ATOM   2852 C  CB   A ASP   A 1 135 ? 12.017 -7.861  -8.454  0.70 17.54 ?  135 ASP   A CB   1 
ATOM   2853 C  CB   B ASP   A 1 135 ? 11.668 -7.422  -8.143  0.30 15.48 ?  135 ASP   A CB   1 
ATOM   2854 C  CG   A ASP   A 1 135 ? 10.709 -8.468  -7.950  0.70 19.33 ?  135 ASP   A CG   1 
ATOM   2855 C  CG   B ASP   A 1 135 ? 10.236 -7.713  -7.722  0.30 16.60 ?  135 ASP   A CG   1 
ATOM   2856 O  OD1  A ASP   A 1 135 ? 10.167 -8.027  -6.916  0.70 19.30 ?  135 ASP   A OD1  1 
ATOM   2857 O  OD1  B ASP   A 1 135 ? 9.865  -7.376  -6.577  0.30 17.03 ?  135 ASP   A OD1  1 
ATOM   2858 O  OD2  A ASP   A 1 135 ? 10.215 -9.401  -8.613  0.70 21.82 -1 135 ASP   A OD2  1 
ATOM   2859 O  OD2  B ASP   A 1 135 ? 9.487  -8.297  -8.535  0.30 17.38 -1 135 ASP   A OD2  1 
ATOM   2860 H  H    A ASP   A 1 135 ? 14.130 -6.744  -8.721  0.70 17.68 ?  135 ASP   A H    1 
ATOM   2861 H  H    B ASP   A 1 135 ? 13.827 -6.461  -8.564  0.30 16.76 ?  135 ASP   A H    1 
ATOM   2862 H  HA   A ASP   A 1 135 ? 11.835 -5.975  -7.657  0.70 18.55 ?  135 ASP   A HA   1 
ATOM   2863 H  HA   B ASP   A 1 135 ? 11.698 -5.542  -7.323  0.30 17.17 ?  135 ASP   A HA   1 
ATOM   2864 H  HB2  A ASP   A 1 135 ? 11.860 -7.564  -9.360  0.70 21.03 ?  135 ASP   A HB2  1 
ATOM   2865 H  HB2  B ASP   A 1 135 ? 11.690 -7.180  -9.084  0.30 18.56 ?  135 ASP   A HB2  1 
ATOM   2866 H  HB3  A ASP   A 1 135 ? 12.696 -8.553  -8.440  0.70 21.03 ?  135 ASP   A HB3  1 
ATOM   2867 H  HB3  B ASP   A 1 135 ? 12.168 -8.238  -7.999  0.30 18.56 ?  135 ASP   A HB3  1 
ATOM   2868 N  N    A PRO   A 1 136 ? 12.062 -6.504  -5.196  0.70 14.38 ?  136 PRO   A N    1 
ATOM   2869 N  N    B PRO   A 1 136 ? 12.027 -6.138  -4.886  0.30 13.08 ?  136 PRO   A N    1 
ATOM   2870 C  CA   A PRO   A 1 136 ? 12.295 -6.909  -3.798  0.70 14.52 ?  136 PRO   A CA   1 
ATOM   2871 C  CA   B PRO   A 1 136 ? 12.289 -6.589  -3.509  0.30 13.12 ?  136 PRO   A CA   1 
ATOM   2872 C  C    A PRO   A 1 136 ? 11.877 -8.335  -3.487  0.70 13.83 ?  136 PRO   A C    1 
ATOM   2873 C  C    B PRO   A 1 136 ? 11.847 -8.017  -3.229  0.30 12.72 ?  136 PRO   A C    1 
ATOM   2874 O  O    A PRO   A 1 136 ? 12.487 -8.969  -2.618  0.70 13.50 ?  136 PRO   A O    1 
ATOM   2875 O  O    B PRO   A 1 136 ? 12.406 -8.664  -2.334  0.30 11.80 ?  136 PRO   A O    1 
ATOM   2876 C  CB   A PRO   A 1 136 ? 11.490 -5.879  -2.994  0.70 15.11 ?  136 PRO   A CB   1 
ATOM   2877 C  CB   B PRO   A 1 136 ? 11.528 -5.562  -2.655  0.30 13.60 ?  136 PRO   A CB   1 
ATOM   2878 C  CG   A PRO   A 1 136 ? 10.449 -5.381  -3.951  0.70 15.62 ?  136 PRO   A CG   1 
ATOM   2879 C  CG   B PRO   A 1 136 ? 10.531 -4.948  -3.593  0.30 13.83 ?  136 PRO   A CG   1 
ATOM   2880 C  CD   A PRO   A 1 136 ? 11.078 -5.411  -5.305  0.70 15.01 ?  136 PRO   A CD   1 
ATOM   2881 C  CD   B PRO   A 1 136 ? 11.185 -4.933  -4.924  0.30 13.32 ?  136 PRO   A CD   1 
ATOM   2882 H  HA   A PRO   A 1 136 ? 13.235 -6.810  -3.573  0.70 17.41 ?  136 PRO   A HA   1 
ATOM   2883 H  HA   B PRO   A 1 136 ? 13.236 -6.511  -3.311  0.30 15.73 ?  136 PRO   A HA   1 
ATOM   2884 H  HB2  A PRO   A 1 136 ? 11.077 -6.309  -2.227  0.70 18.12 ?  136 PRO   A HB2  1 
ATOM   2885 H  HB2  B PRO   A 1 136 ? 11.079 -6.009  -1.923  0.30 16.31 ?  136 PRO   A HB2  1 
ATOM   2886 H  HB3  A PRO   A 1 136 ? 12.075 -5.158  -2.709  0.70 18.12 ?  136 PRO   A HB3  1 
ATOM   2887 H  HB3  B PRO   A 1 136 ? 12.144 -4.887  -2.323  0.30 16.31 ?  136 PRO   A HB3  1 
ATOM   2888 H  HG2  A PRO   A 1 136 ? 9.679  -5.964  -3.921  0.70 18.73 ?  136 PRO   A HG2  1 
ATOM   2889 H  HG2  B PRO   A 1 136 ? 9.731  -5.495  -3.623  0.30 16.57 ?  136 PRO   A HG2  1 
ATOM   2890 H  HG3  A PRO   A 1 136 ? 10.204 -4.474  -3.714  0.70 18.73 ?  136 PRO   A HG3  1 
ATOM   2891 H  HG3  B PRO   A 1 136 ? 10.322 -4.047  -3.310  0.30 16.57 ?  136 PRO   A HG3  1 
ATOM   2892 H  HD2  A PRO   A 1 136 ? 10.413 -5.627  -5.980  0.70 17.99 ?  136 PRO   A HD2  1 
ATOM   2893 H  HD2  B PRO   A 1 136 ? 10.520 -5.005  -5.628  0.30 15.97 ?  136 PRO   A HD2  1 
ATOM   2894 H  HD3  A PRO   A 1 136 ? 11.523 -4.573  -5.498  0.70 17.99 ?  136 PRO   A HD3  1 
ATOM   2895 H  HD3  B PRO   A 1 136 ? 11.734 -4.139  -5.033  0.30 15.97 ?  136 PRO   A HD3  1 
ATOM   2896 N  N    A ILE   A 1 137 ? 10.837 -8.854  -4.141  0.70 13.74 ?  137 ILE   A N    1 
ATOM   2897 N  N    B ILE   A 1 137 ? 10.855 -8.530  -3.961  0.30 13.16 ?  137 ILE   A N    1 
ATOM   2898 C  CA   A ILE   A 1 137 ? 10.468 -10.252 -3.939  0.70 14.04 ?  137 ILE   A CA   1 
ATOM   2899 C  CA   B ILE   A 1 137 ? 10.436 -9.918  -3.772  0.30 13.55 ?  137 ILE   A CA   1 
ATOM   2900 C  C    A ILE   A 1 137 ? 11.629 -11.155 -4.329  0.70 13.82 ?  137 ILE   A C    1 
ATOM   2901 C  C    B ILE   A 1 137 ? 11.565 -10.867 -4.158  0.30 13.51 ?  137 ILE   A C    1 
ATOM   2902 O  O    A ILE   A 1 137 ? 11.944 -12.129 -3.633  0.70 14.01 ?  137 ILE   A O    1 
ATOM   2903 O  O    B ILE   A 1 137 ? 11.855 -11.838 -3.448  0.30 13.51 ?  137 ILE   A O    1 
ATOM   2904 C  CB   A ILE   A 1 137 ? 9.183  -10.586 -4.719  0.70 14.99 ?  137 ILE   A CB   1 
ATOM   2905 C  CB   B ILE   A 1 137 ? 9.153  -10.206 -4.574  0.30 14.27 ?  137 ILE   A CB   1 
ATOM   2906 C  CG1  A ILE   A 1 137 ? 7.998  -9.773  -4.181  0.70 16.72 ?  137 ILE   A CG1  1 
ATOM   2907 C  CG1  B ILE   A 1 137 ? 8.060  -9.178  -4.251  0.30 15.43 ?  137 ILE   A CG1  1 
ATOM   2908 C  CG2  A ILE   A 1 137 ? 8.897  -12.081 -4.651  0.70 15.64 ?  137 ILE   A CG2  1 
ATOM   2909 C  CG2  B ILE   A 1 137 ? 8.667  -11.627 -4.301  0.30 14.31 ?  137 ILE   A CG2  1 
ATOM   2910 C  CD1  A ILE   A 1 137 ? 6.724  -9.934  -4.984  0.70 18.30 ?  137 ILE   A CD1  1 
ATOM   2911 C  CD1  B ILE   A 1 137 ? 6.843  -9.290  -5.142  0.30 16.16 ?  137 ILE   A CD1  1 
ATOM   2912 H  H    A ILE   A 1 137 ? 10.345 -8.430  -4.696  0.70 16.47 ?  137 ILE   A H    1 
ATOM   2913 H  H    B ILE   A 1 137 ? 10.417 -8.097  -4.562  0.30 15.78 ?  137 ILE   A H    1 
ATOM   2914 H  HA   A ILE   A 1 137 ? 10.291 -10.404 -3.000  0.70 16.84 ?  137 ILE   A HA   1 
ATOM   2915 H  HA   B ILE   A 1 137 ? 10.234 -10.057 -2.834  0.30 16.25 ?  137 ILE   A HA   1 
ATOM   2916 H  HB   A ILE   A 1 137 ? 9.316  -10.349 -5.648  0.70 17.97 ?  137 ILE   A HB   1 
ATOM   2917 H  HB   B ILE   A 1 137 ? 9.362  -10.133 -5.516  0.30 17.10 ?  137 ILE   A HB   1 
ATOM   2918 H  HG12 A ILE   A 1 137 ? 7.816  -10.050 -3.270  0.70 20.05 ?  137 ILE   A HG12 1 
ATOM   2919 H  HG12 B ILE   A 1 137 ? 7.771  -9.303  -3.335  0.30 18.50 ?  137 ILE   A HG12 1 
ATOM   2920 H  HG13 A ILE   A 1 137 ? 8.239  -8.831  -4.194  0.70 20.05 ?  137 ILE   A HG13 1 
ATOM   2921 H  HG13 B ILE   A 1 137 ? 8.416  -8.281  -4.363  0.30 18.50 ?  137 ILE   A HG13 1 
ATOM   2922 H  HG21 A ILE   A 1 137 ? 7.979  -12.258 -4.919  0.70 18.75 ?  137 ILE   A HG21 1 
ATOM   2923 H  HG21 B ILE   A 1 137 ? 7.816  -11.764 -4.745  0.30 17.16 ?  137 ILE   A HG21 1 
ATOM   2924 H  HG22 A ILE   A 1 137 ? 9.500  -12.546 -5.250  0.70 18.75 ?  137 ILE   A HG22 1 
ATOM   2925 H  HG22 B ILE   A 1 137 ? 9.321  -12.255 -4.644  0.30 17.16 ?  137 ILE   A HG22 1 
ATOM   2926 H  HG23 A ILE   A 1 137 ? 9.031  -12.386 -3.742  0.70 18.75 ?  137 ILE   A HG23 1 
ATOM   2927 H  HG23 B ILE   A 1 137 ? 8.563  -11.746 -3.344  0.30 17.16 ?  137 ILE   A HG23 1 
ATOM   2928 H  HD11 A ILE   A 1 137 ? 5.999  -10.155 -4.381  0.70 21.94 ?  137 ILE   A HD11 1 
ATOM   2929 H  HD11 B ILE   A 1 137 ? 6.619  -8.410  -5.484  0.30 19.38 ?  137 ILE   A HD11 1 
ATOM   2930 H  HD12 A ILE   A 1 137 ? 6.544  -9.100  -5.437  0.70 21.94 ?  137 ILE   A HD12 1 
ATOM   2931 H  HD12 B ILE   A 1 137 ? 7.045  -9.888  -5.878  0.30 19.38 ?  137 ILE   A HD12 1 
ATOM   2932 H  HD13 A ILE   A 1 137 ? 6.840  -10.640 -5.639  0.70 21.94 ?  137 ILE   A HD13 1 
ATOM   2933 H  HD13 B ILE   A 1 137 ? 6.104  -9.645  -4.623  0.30 19.38 ?  137 ILE   A HD13 1 
ATOM   2934 N  N    A HIS   A 1 138 ? 12.289 -10.836 -5.442  0.70 14.24 ?  138 HIS   A N    1 
ATOM   2935 N  N    B HIS   A 1 138 ? 12.214 -10.600 -5.294  0.30 13.68 ?  138 HIS   A N    1 
ATOM   2936 C  CA   A HIS   A 1 138 ? 13.487 -11.566 -5.830  0.70 14.31 ?  138 HIS   A CA   1 
ATOM   2937 C  CA   B HIS   A 1 138 ? 13.321 -11.437 -5.751  0.30 13.50 ?  138 HIS   A CA   1 
ATOM   2938 C  C    A HIS   A 1 138 ? 14.609 -11.382 -4.811  0.70 13.81 ?  138 HIS   A C    1 
ATOM   2939 C  C    B HIS   A 1 138 ? 14.503 -11.360 -4.791  0.30 13.34 ?  138 HIS   A C    1 
ATOM   2940 O  O    A HIS   A 1 138 ? 15.294 -12.350 -4.456  0.70 14.14 ?  138 HIS   A O    1 
ATOM   2941 O  O    B HIS   A 1 138 ? 15.128 -12.379 -4.474  0.30 13.53 ?  138 HIS   A O    1 
ATOM   2942 C  CB   A HIS   A 1 138 ? 13.929 -11.140 -7.227  0.70 15.54 ?  138 HIS   A CB   1 
ATOM   2943 C  CB   B HIS   A 1 138 ? 13.727 -10.996 -7.158  0.30 13.55 ?  138 HIS   A CB   1 
ATOM   2944 C  CG   A HIS   A 1 138 ? 15.173 -11.828 -7.691  0.70 16.44 ?  138 HIS   A CG   1 
ATOM   2945 C  CG   B HIS   A 1 138 ? 15.034 -11.561 -7.620  0.30 13.62 ?  138 HIS   A CG   1 
ATOM   2946 N  ND1  A HIS   A 1 138 ? 15.236 -13.188 -7.901  0.70 17.77 ?  138 HIS   A ND1  1 
ATOM   2947 N  ND1  B HIS   A 1 138 ? 15.192 -12.885 -7.966  0.30 14.26 ?  138 HIS   A ND1  1 
ATOM   2948 C  CD2  A HIS   A 1 138 ? 16.407 -11.345 -7.961  0.70 16.76 ?  138 HIS   A CD2  1 
ATOM   2949 C  CD2  B HIS   A 1 138 ? 16.243 -10.978 -7.800  0.30 13.41 ?  138 HIS   A CD2  1 
ATOM   2950 C  CE1  A HIS   A 1 138 ? 16.454 -13.512 -8.295  0.70 18.09 ?  138 HIS   A CE1  1 
ATOM   2951 C  CE1  B HIS   A 1 138 ? 16.444 -13.094 -8.335  0.30 14.15 ?  138 HIS   A CE1  1 
ATOM   2952 N  NE2  A HIS   A 1 138 ? 17.186 -12.413 -8.339  0.70 17.40 ?  138 HIS   A NE2  1 
ATOM   2953 N  NE2  B HIS   A 1 138 ? 17.103 -11.953 -8.244  0.30 13.75 ?  138 HIS   A NE2  1 
ATOM   2954 H  H    A HIS   A 1 138 ? 12.056 -10.211 -5.989  0.70 17.07 ?  138 HIS   A H    1 
ATOM   2955 H  H    B HIS   A 1 138 ? 12.033 -9.938  -5.814  0.30 16.40 ?  138 HIS   A H    1 
ATOM   2956 H  HA   A HIS   A 1 138 ? 13.274 -12.509 -5.870  0.70 17.16 ?  138 HIS   A HA   1 
ATOM   2957 H  HA   B HIS   A 1 138 ? 13.025 -12.358 -5.796  0.30 16.19 ?  138 HIS   A HA   1 
ATOM   2958 H  HB2  A HIS   A 1 138 ? 13.216 -11.350 -7.859  0.70 18.64 ?  138 HIS   A HB2  1 
ATOM   2959 H  HB2  B HIS   A 1 138 ? 13.041 -11.283 -7.785  0.30 16.24 ?  138 HIS   A HB2  1 
ATOM   2960 H  HB3  A HIS   A 1 138 ? 14.093 -10.185 -7.230  0.70 18.64 ?  138 HIS   A HB3  1 
ATOM   2961 H  HB3  B HIS   A 1 138 ? 13.799 -10.029 -7.176  0.30 16.24 ?  138 HIS   A HB3  1 
ATOM   2962 H  HD1  A HIS   A 1 138 ? 14.578 -13.738 -7.799  0.70 21.30 ?  138 HIS   A HD1  1 
ATOM   2963 H  HD1  B HIS   A 1 138 ? 14.571 -13.482 -7.942  0.30 17.09 ?  138 HIS   A HD1  1 
ATOM   2964 H  HD2  A HIS   A 1 138 ? 16.670 -10.455 -7.904  0.70 20.10 ?  138 HIS   A HD2  1 
ATOM   2965 H  HD2  B HIS   A 1 138 ? 16.451 -10.084 -7.650  0.30 16.08 ?  138 HIS   A HD2  1 
ATOM   2966 H  HE1  A HIS   A 1 138 ? 16.745 -14.367 -8.500  0.70 21.69 ?  138 HIS   A HE1  1 
ATOM   2967 H  HE1  B HIS   A 1 138 ? 16.797 -13.908 -8.610  0.30 16.96 ?  138 HIS   A HE1  1 
ATOM   2968 N  N    . SER   A 1 139 ? 14.817 -10.154 -4.321  1.00 13.02 ?  139 SER   A N    1 
ATOM   2969 C  CA   . SER   A 1 139 ? 15.888 -9.960  -3.352  1.00 12.96 ?  139 SER   A CA   1 
ATOM   2970 C  C    . SER   A 1 139 ? 15.671 -10.795 -2.096  1.00 12.56 ?  139 SER   A C    1 
ATOM   2971 O  O    . SER   A 1 139 ? 16.619 -11.393 -1.574  1.00 12.91 ?  139 SER   A O    1 
ATOM   2972 C  CB   . SER   A 1 139 ? 16.021 -8.480  -3.002  1.00 13.06 ?  139 SER   A CB   1 
ATOM   2973 O  OG   . SER   A 1 139 ? 17.100 -8.300  -2.104  1.00 13.32 ?  139 SER   A OG   1 
ATOM   2974 H  H    A SER   A 1 139 ? 14.372 -9.448  -4.527  0.70 15.61 ?  139 SER   A H    1 
ATOM   2975 H  H    B SER   A 1 139 ? 14.414 -9.429  -4.546  0.30 15.61 ?  139 SER   A H    1 
ATOM   2976 H  HA   . SER   A 1 139 ? 16.726 -10.242 -3.752  1.00 15.54 ?  139 SER   A HA   1 
ATOM   2977 H  HB2  . SER   A 1 139 ? 16.193 -7.970  -3.810  1.00 15.65 ?  139 SER   A HB2  1 
ATOM   2978 H  HB3  . SER   A 1 139 ? 15.200 -8.174  -2.582  1.00 15.65 ?  139 SER   A HB3  1 
ATOM   2979 H  HG   . SER   A 1 139 ? 17.180 -7.485  -1.901  1.00 15.97 ?  139 SER   A HG   1 
ATOM   2980 N  N    A LEU   A 1 140 ? 14.421 -10.914 -1.646  0.70 12.43 ?  140 LEU   A N    1 
ATOM   2981 N  N    B LEU   A 1 140 ? 14.459 -10.747 -1.529  0.30 11.74 ?  140 LEU   A N    1 
ATOM   2982 C  CA   A LEU   A 1 140 ? 14.150 -11.751 -0.482  0.70 12.39 ?  140 LEU   A CA   1 
ATOM   2983 C  CA   B LEU   A 1 140 ? 14.177 -11.527 -0.326  0.30 11.16 ?  140 LEU   A CA   1 
ATOM   2984 C  C    A LEU   A 1 140 ? 14.444 -13.219 -0.772  0.70 12.43 ?  140 LEU   A C    1 
ATOM   2985 C  C    B LEU   A 1 140 ? 14.377 -13.012 -0.593  0.30 11.71 ?  140 LEU   A C    1 
ATOM   2986 O  O    A LEU   A 1 140 ? 15.033 -13.916 0.064   0.70 12.91 ?  140 LEU   A O    1 
ATOM   2987 O  O    B LEU   A 1 140 ? 14.852 -13.754 0.277   0.30 11.88 ?  140 LEU   A O    1 
ATOM   2988 C  CB   A LEU   A 1 140 ? 12.703 -11.560 -0.032  0.70 13.23 ?  140 LEU   A CB   1 
ATOM   2989 C  CB   B LEU   A 1 140 ? 12.748 -11.245 0.155   0.30 10.40 ?  140 LEU   A CB   1 
ATOM   2990 C  CG   A LEU   A 1 140 ? 12.263 -12.440 1.137   0.70 13.74 ?  140 LEU   A CG   1 
ATOM   2991 C  CG   B LEU   A 1 140 ? 12.205 -12.086 1.316   0.30 10.20 ?  140 LEU   A CG   1 
ATOM   2992 C  CD1  A LEU   A 1 140 ? 13.151 -12.227 2.354   0.70 14.35 ?  140 LEU   A CD1  1 
ATOM   2993 C  CD1  B LEU   A 1 140 ? 13.095 -11.961 2.537   0.30 9.96  ?  140 LEU   A CD1  1 
ATOM   2994 C  CD2  A LEU   A 1 140 ? 10.802 -12.176 1.479   0.70 13.80 ?  140 LEU   A CD2  1 
ATOM   2995 C  CD2  B LEU   A 1 140 ? 10.768 -11.692 1.659   0.30 10.54 ?  140 LEU   A CD2  1 
ATOM   2996 H  H    A LEU   A 1 140 ? 13.732 -10.531 -1.989  0.70 14.90 ?  140 LEU   A H    1 
ATOM   2997 H  H    B LEU   A 1 140 ? 13.802 -10.267 -1.813  0.30 14.07 ?  140 LEU   A H    1 
ATOM   2998 H  HA   A LEU   A 1 140 ? 14.726 -11.475 0.242   0.70 14.86 ?  140 LEU   A HA   1 
ATOM   2999 H  HA   B LEU   A 1 140 ? 14.787 -11.252 0.378   0.30 13.38 ?  140 LEU   A HA   1 
ATOM   3000 H  HB2  A LEU   A 1 140 ? 12.584 -10.640 0.238   0.70 15.86 ?  140 LEU   A HB2  1 
ATOM   3001 H  HB2  B LEU   A 1 140 ? 12.701 -10.318 0.437   0.30 12.46 ?  140 LEU   A HB2  1 
ATOM   3002 H  HB3  A LEU   A 1 140 ? 12.118 -11.760 -0.781  0.70 15.86 ?  140 LEU   A HB3  1 
ATOM   3003 H  HB3  B LEU   A 1 140 ? 12.148 -11.380 -0.593  0.30 12.46 ?  140 LEU   A HB3  1 
ATOM   3004 H  HG   A LEU   A 1 140 ? 12.336 -13.373 0.876   0.70 16.47 ?  140 LEU   A HG   1 
ATOM   3005 H  HG   B LEU   A 1 140 ? 12.194 -13.019 1.051   0.30 12.23 ?  140 LEU   A HG   1 
ATOM   3006 H  HD11 A LEU   A 1 140 ? 12.773 -12.708 3.106   0.70 17.21 ?  140 LEU   A HD11 1 
ATOM   3007 H  HD11 B LEU   A 1 140 ? 12.694 -12.456 3.269   0.30 11.94 ?  140 LEU   A HD11 1 
ATOM   3008 H  HD12 A LEU   A 1 140 ? 14.040 -12.564 2.159   0.70 17.21 ?  140 LEU   A HD12 1 
ATOM   3009 H  HD12 B LEU   A 1 140 ? 13.966 -12.330 2.326   0.30 11.94 ?  140 LEU   A HD12 1 
ATOM   3010 H  HD13 A LEU   A 1 140 ? 13.190 -11.279 2.552   0.70 17.21 ?  140 LEU   A HD13 1 
ATOM   3011 H  HD13 B LEU   A 1 140 ? 13.175 -11.026 2.772   0.30 11.94 ?  140 LEU   A HD13 1 
ATOM   3012 H  HD21 A LEU   A 1 140 ? 10.542 -12.744 2.222   0.70 16.54 ?  140 LEU   A HD21 1 
ATOM   3013 H  HD21 B LEU   A 1 140 ? 10.447 -12.258 2.381   0.30 12.64 ?  140 LEU   A HD21 1 
ATOM   3014 H  HD22 A LEU   A 1 140 ? 10.698 -11.243 1.725   0.70 16.54 ?  140 LEU   A HD22 1 
ATOM   3015 H  HD22 B LEU   A 1 140 ? 10.750 -10.763 1.937   0.30 12.64 ?  140 LEU   A HD22 1 
ATOM   3016 H  HD23 A LEU   A 1 140 ? 10.253 -12.376 0.703   0.70 16.54 ?  140 LEU   A HD23 1 
ATOM   3017 H  HD23 B LEU   A 1 140 ? 10.209 -11.814 0.874   0.30 12.64 ?  140 LEU   A HD23 1 
ATOM   3018 N  N    A ARG   A 1 141 ? 14.039 -13.706 -1.948  0.70 12.79 ?  141 ARG   A N    1 
ATOM   3019 N  N    B ARG   A 1 141 ? 14.027 -13.457 -1.800  0.30 12.49 ?  141 ARG   A N    1 
ATOM   3020 C  CA   A ARG   A 1 141 ? 14.305 -15.094 -2.313  0.70 13.78 ?  141 ARG   A CA   1 
ATOM   3021 C  CA   B ARG   A 1 141 ? 14.225 -14.851 -2.178  0.30 13.48 ?  141 ARG   A CA   1 
ATOM   3022 C  C    A ARG   A 1 141 ? 15.804 -15.382 -2.307  0.70 13.26 ?  141 ARG   A C    1 
ATOM   3023 C  C    B ARG   A 1 141 ? 15.710 -15.197 -2.228  0.30 13.18 ?  141 ARG   A C    1 
ATOM   3024 O  O    A ARG   A 1 141 ? 16.255 -16.394 -1.756  0.70 13.38 ?  141 ARG   A O    1 
ATOM   3025 O  O    B ARG   A 1 141 ? 16.141 -16.220 -1.682  0.30 13.58 ?  141 ARG   A O    1 
ATOM   3026 C  CB   A ARG   A 1 141 ? 13.707 -15.370 -3.696  0.70 14.89 ?  141 ARG   A CB   1 
ATOM   3027 C  CB   B ARG   A 1 141 ? 13.566 -15.096 -3.537  0.30 14.83 ?  141 ARG   A CB   1 
ATOM   3028 C  CG   A ARG   A 1 141 ? 13.705 -16.817 -4.119  0.70 16.28 ?  141 ARG   A CG   1 
ATOM   3029 C  CG   B ARG   A 1 141 ? 13.196 -16.539 -3.817  0.30 16.46 ?  141 ARG   A CG   1 
ATOM   3030 C  CD   A ARG   A 1 141 ? 12.660 -17.559 -3.352  0.70 17.85 ?  141 ARG   A CD   1 
ATOM   3031 C  CD   B ARG   A 1 141 ? 11.815 -16.866 -3.265  0.30 17.75 ?  141 ARG   A CD   1 
ATOM   3032 N  NE   A ARG   A 1 141 ? 13.265 -18.299 -2.261  0.70 18.83 ?  141 ARG   A NE   1 
ATOM   3033 N  NE   B ARG   A 1 141 ? 11.875 -17.852 -2.194  0.30 17.68 ?  141 ARG   A NE   1 
ATOM   3034 C  CZ   A ARG   A 1 141 ? 12.586 -18.865 -1.273  0.70 19.71 ?  141 ARG   A CZ   1 
ATOM   3035 C  CZ   B ARG   A 1 141 ? 10.837 -18.238 -1.467  0.30 17.37 ?  141 ARG   A CZ   1 
ATOM   3036 N  NH1  A ARG   A 1 141 ? 11.295 -18.644 -1.106  0.70 19.35 ?  141 ARG   A NH1  1 
ATOM   3037 N  NH1  B ARG   A 1 141 ? 9.629  -17.731 -1.657  0.30 17.12 ?  141 ARG   A NH1  1 
ATOM   3038 N  NH2  A ARG   A 1 141 ? 13.223 -19.663 -0.422  0.70 20.58 ?  141 ARG   A NH2  1 
ATOM   3039 N  NH2  B ARG   A 1 141 ? 11.013 -19.160 -0.526  0.30 17.77 ?  141 ARG   A NH2  1 
ATOM   3040 H  H    A ARG   A 1 141 ? 13.615 -13.261 -2.549  0.70 15.33 ?  141 ARG   A H    1 
ATOM   3041 H  H    B ARG   A 1 141 ? 13.668 -12.969 -2.409  0.30 14.97 ?  141 ARG   A H    1 
ATOM   3042 H  HA   A ARG   A 1 141 ? 13.880 -15.688 -1.675  0.70 16.52 ?  141 ARG   A HA   1 
ATOM   3043 H  HA   B ARG   A 1 141 ? 13.803 -15.424 -1.524  0.30 16.16 ?  141 ARG   A HA   1 
ATOM   3044 H  HB2  A ARG   A 1 141 ? 12.793 -15.058 -3.708  0.70 17.85 ?  141 ARG   A HB2  1 
ATOM   3045 H  HB2  B ARG   A 1 141 ? 12.757 -14.560 -3.592  0.30 17.78 ?  141 ARG   A HB2  1 
ATOM   3046 H  HB3  A ARG   A 1 141 ? 14.226 -14.884 -4.355  0.70 17.85 ?  141 ARG   A HB3  1 
ATOM   3047 H  HB3  B ARG   A 1 141 ? 14.182 -14.816 -4.230  0.30 17.78 ?  141 ARG   A HB3  1 
ATOM   3048 H  HG2  A ARG   A 1 141 ? 13.500 -16.885 -5.067  0.70 19.52 ?  141 ARG   A HG2  1 
ATOM   3049 H  HG2  B ARG   A 1 141 ? 13.184 -16.688 -4.777  0.30 19.74 ?  141 ARG   A HG2  1 
ATOM   3050 H  HG3  A ARG   A 1 141 ? 14.571 -17.222 -3.933  0.70 19.52 ?  141 ARG   A HG3  1 
ATOM   3051 H  HG3  B ARG   A 1 141 ? 13.843 -17.126 -3.394  0.30 19.74 ?  141 ARG   A HG3  1 
ATOM   3052 H  HD2  A ARG   A 1 141 ? 12.023 -16.934 -2.971  0.70 21.41 ?  141 ARG   A HD2  1 
ATOM   3053 H  HD2  B ARG   A 1 141 ? 11.407 -16.061 -2.907  0.30 21.28 ?  141 ARG   A HD2  1 
ATOM   3054 H  HD3  A ARG   A 1 141 ? 12.202 -18.182 -3.944  0.70 21.41 ?  141 ARG   A HD3  1 
ATOM   3055 H  HD3  B ARG   A 1 141 ? 11.266 -17.228 -3.976  0.30 21.28 ?  141 ARG   A HD3  1 
ATOM   3056 H  HE   A ARG   A 1 141 ? 14.106 -18.461 -2.309  0.70 22.58 ?  141 ARG   A HE   1 
ATOM   3057 H  HE   B ARG   A 1 141 ? 12.635 -18.219 -2.032  0.30 21.20 ?  141 ARG   A HE   1 
ATOM   3058 H  HH11 A ARG   A 1 141 ? 10.864 -18.147 -1.658  0.70 23.20 ?  141 ARG   A HH11 1 
ATOM   3059 H  HH11 B ARG   A 1 141 ? 9.502  -17.134 -2.264  0.30 20.53 ?  141 ARG   A HH11 1 
ATOM   3060 H  HH12 A ARG   A 1 141 ? 10.875 -19.022 -0.454  0.70 23.20 ?  141 ARG   A HH12 1 
ATOM   3061 H  HH12 B ARG   A 1 141 ? 8.970  -17.998 -1.174  0.30 20.53 ?  141 ARG   A HH12 1 
ATOM   3062 H  HH21 A ARG   A 1 141 ? 14.066 -19.811 -0.519  0.70 24.68 ?  141 ARG   A HH21 1 
ATOM   3063 H  HH21 B ARG   A 1 141 ? 11.794 -19.496 -0.394  0.30 21.31 ?  141 ARG   A HH21 1 
ATOM   3064 H  HH22 A ARG   A 1 141 ? 12.798 -20.024 0.233   0.70 24.68 ?  141 ARG   A HH22 1 
ATOM   3065 H  HH22 B ARG   A 1 141 ? 10.347 -19.420 -0.048  0.30 21.31 ?  141 ARG   A HH22 1 
ATOM   3066 N  N    A VAL   A 1 142 ? 16.594 -14.505 -2.925  0.70 12.71 ?  142 VAL   A N    1 
ATOM   3067 N  N    B VAL   A 1 142 ? 16.513 -14.351 -2.882  0.30 12.74 ?  142 VAL   A N    1 
ATOM   3068 C  CA   A VAL   A 1 142 ? 18.041 -14.705 -2.936  0.70 12.85 ?  142 VAL   A CA   1 
ATOM   3069 C  CA   B VAL   A 1 142 ? 17.952 -14.601 -2.959  0.30 12.48 ?  142 VAL   A CA   1 
ATOM   3070 C  C    A VAL   A 1 142 ? 18.596 -14.660 -1.519  0.70 12.36 ?  142 VAL   A C    1 
ATOM   3071 C  C    B VAL   A 1 142 ? 18.560 -14.634 -1.562  0.30 12.25 ?  142 VAL   A C    1 
ATOM   3072 O  O    A VAL   A 1 142 ? 19.462 -15.466 -1.155  0.70 12.62 ?  142 VAL   A O    1 
ATOM   3073 O  O    B VAL   A 1 142 ? 19.426 -15.465 -1.259  0.30 12.25 ?  142 VAL   A O    1 
ATOM   3074 C  CB   A VAL   A 1 142 ? 18.740 -13.697 -3.867  0.70 13.24 ?  142 VAL   A CB   1 
ATOM   3075 C  CB   B VAL   A 1 142 ? 18.634 -13.552 -3.860  0.30 12.60 ?  142 VAL   A CB   1 
ATOM   3076 C  CG1  A VAL   A 1 142 ? 20.253 -13.919 -3.832  0.70 13.01 ?  142 VAL   A CG1  1 
ATOM   3077 C  CG1  B VAL   A 1 142 ? 20.147 -13.723 -3.827  0.30 12.74 ?  142 VAL   A CG1  1 
ATOM   3078 C  CG2  A VAL   A 1 142 ? 18.234 -13.835 -5.291  0.70 14.54 ?  142 VAL   A CG2  1 
ATOM   3079 C  CG2  B VAL   A 1 142 ? 18.128 -13.664 -5.287  0.30 13.07 ?  142 VAL   A CG2  1 
ATOM   3080 H  H    A VAL   A 1 142 ? 16.326 -13.802 -3.341  0.70 15.23 ?  142 VAL   A H    1 
ATOM   3081 H  H    B VAL   A 1 142 ? 16.253 -13.630 -3.283  0.30 15.27 ?  142 VAL   A H    1 
ATOM   3082 H  HA   A VAL   A 1 142 ? 18.228 -15.587 -3.290  0.70 15.41 ?  142 VAL   A HA   1 
ATOM   3083 H  HA   B VAL   A 1 142 ? 18.096 -15.465 -3.367  0.30 14.96 ?  142 VAL   A HA   1 
ATOM   3084 H  HB   A VAL   A 1 142 ? 18.563 -12.791 -3.566  0.70 15.87 ?  142 VAL   A HB   1 
ATOM   3085 H  HB   B VAL   A 1 142 ? 18.427 -12.659 -3.537  0.30 15.10 ?  142 VAL   A HB   1 
ATOM   3086 H  HG11 A VAL   A 1 142 ? 20.663 -13.433 -4.567  0.70 15.60 ?  142 VAL   A HG11 1 
ATOM   3087 H  HG11 B VAL   A 1 142 ? 20.540 -13.197 -4.544  0.30 15.27 ?  142 VAL   A HG11 1 
ATOM   3088 H  HG12 A VAL   A 1 142 ? 20.606 -13.593 -2.989  0.70 15.60 ?  142 VAL   A HG12 1 
ATOM   3089 H  HG12 B VAL   A 1 142 ? 20.486 -13.415 -2.972  0.30 15.27 ?  142 VAL   A HG12 1 
ATOM   3090 H  HG13 A VAL   A 1 142 ? 20.436 -14.867 -3.925  0.70 15.60 ?  142 VAL   A HG13 1 
ATOM   3091 H  HG13 B VAL   A 1 142 ? 20.361 -14.659 -3.953  0.30 15.27 ?  142 VAL   A HG13 1 
ATOM   3092 H  HG21 A VAL   A 1 142 ? 18.719 -13.215 -5.861  0.70 17.43 ?  142 VAL   A HG21 1 
ATOM   3093 H  HG21 B VAL   A 1 142 ? 18.569 -12.992 -5.833  0.30 15.66 ?  142 VAL   A HG21 1 
ATOM   3094 H  HG22 A VAL   A 1 142 ? 18.389 -14.745 -5.591  0.70 17.43 ?  142 VAL   A HG22 1 
ATOM   3095 H  HG22 B VAL   A 1 142 ? 18.336 -14.549 -5.624  0.30 15.66 ?  142 VAL   A HG22 1 
ATOM   3096 H  HG23 A VAL   A 1 142 ? 17.289 -13.633 -5.309  0.70 17.43 ?  142 VAL   A HG23 1 
ATOM   3097 H  HG23 B VAL   A 1 142 ? 17.172 -13.520 -5.294  0.30 15.66 ?  142 VAL   A HG23 1 
ATOM   3098 N  N    . CYS   A 1 143 ? 18.114 -13.726 -0.695  1.00 12.30 ?  143 CYS   A N    1 
ATOM   3099 C  CA   . CYS   A 1 143 ? 18.578 -13.680 0.687   1.00 12.68 ?  143 CYS   A CA   1 
ATOM   3100 C  C    . CYS   A 1 143 ? 18.347 -15.018 1.381   1.00 12.77 ?  143 CYS   A C    1 
ATOM   3101 O  O    . CYS   A 1 143 ? 19.265 -15.605 1.959   1.00 12.75 ?  143 CYS   A O    1 
ATOM   3102 C  CB   . CYS   A 1 143 ? 17.850 -12.563 1.430   1.00 12.71 ?  143 CYS   A CB   1 
ATOM   3103 S  SG   . CYS   A 1 143 ? 18.338 -12.379 3.153   1.00 13.44 ?  143 CYS   A SG   1 
ATOM   3104 H  H    A CYS   A 1 143 ? 17.535 -13.129 -0.906  0.70 14.74 ?  143 CYS   A H    1 
ATOM   3105 H  H    B CYS   A 1 143 ? 17.535 -13.123 -0.886  0.30 14.74 ?  143 CYS   A H    1 
ATOM   3106 H  HA   . CYS   A 1 143 ? 19.529 -13.495 0.703   1.00 15.20 ?  143 CYS   A HA   1 
ATOM   3107 H  HB2  . CYS   A 1 143 ? 18.022 -11.724 0.976   1.00 15.24 ?  143 CYS   A HB2  1 
ATOM   3108 H  HB3  . CYS   A 1 143 ? 16.900 -12.751 1.414   1.00 15.24 ?  143 CYS   A HB3  1 
ATOM   3109 H  HG   . CYS   A 1 143 ? 17.744 -11.449 3.621   1.00 16.11 ?  143 CYS   A HG   1 
ATOM   3110 N  N    . VAL   A 1 144 ? 17.114 -15.518 1.325   1.00 13.37 ?  144 VAL   A N    1 
ATOM   3111 C  CA   . VAL   A 1 144 ? 16.772 -16.750 2.023   1.00 14.45 ?  144 VAL   A CA   1 
ATOM   3112 C  C    . VAL   A 1 144 ? 17.588 -17.924 1.498   1.00 13.92 ?  144 VAL   A C    1 
ATOM   3113 O  O    . VAL   A 1 144 ? 17.951 -18.834 2.257   1.00 14.69 ?  144 VAL   A O    1 
ATOM   3114 C  CB   . VAL   A 1 144 ? 15.256 -16.990 1.896   1.00 17.08 ?  144 VAL   A CB   1 
ATOM   3115 C  CG1  . VAL   A 1 144 ? 14.896 -18.422 2.239   1.00 19.04 ?  144 VAL   A CG1  1 
ATOM   3116 C  CG2  . VAL   A 1 144 ? 14.495 -15.989 2.765   1.00 17.05 ?  144 VAL   A CG2  1 
ATOM   3117 H  H    . VAL   A 1 144 ? 16.459 -15.160 0.886   1.00 16.03 ?  144 VAL   A H    1 
ATOM   3118 H  HA   . VAL   A 1 144 ? 16.970 -16.642 2.960   1.00 17.33 ?  144 VAL   A HA   1 
ATOM   3119 H  HB   . VAL   A 1 144 ? 14.988 -16.831 0.972   1.00 20.48 ?  144 VAL   A HB   1 
ATOM   3120 H  HG11 . VAL   A 1 144 ? 13.944 -18.471 2.428   1.00 22.83 ?  144 VAL   A HG11 1 
ATOM   3121 H  HG12 . VAL   A 1 144 ? 15.110 -18.994 1.486   1.00 22.83 ?  144 VAL   A HG12 1 
ATOM   3122 H  HG13 . VAL   A 1 144 ? 15.399 -18.692 3.021   1.00 22.83 ?  144 VAL   A HG13 1 
ATOM   3123 H  HG21 . VAL   A 1 144 ? 13.538 -16.153 2.686   1.00 20.44 ?  144 VAL   A HG21 1 
ATOM   3124 H  HG22 . VAL   A 1 144 ? 14.768 -16.091 3.689   1.00 20.44 ?  144 VAL   A HG22 1 
ATOM   3125 H  HG23 . VAL   A 1 144 ? 14.691 -15.083 2.463   1.00 20.44 ?  144 VAL   A HG23 1 
ATOM   3126 N  N    . ASP   A 1 145 ? 17.857 -17.946 0.195   1.00 14.12 ?  145 ASP   A N    1 
ATOM   3127 C  CA   . ASP   A 1 145 ? 18.570 -19.053 -0.433  1.00 14.48 ?  145 ASP   A CA   1 
ATOM   3128 C  C    . ASP   A 1 145 ? 20.090 -18.909 -0.383  1.00 14.39 ?  145 ASP   A C    1 
ATOM   3129 O  O    . ASP   A 1 145 ? 20.793 -19.803 -0.863  1.00 16.52 ?  145 ASP   A O    1 
ATOM   3130 C  CB   . ASP   A 1 145 ? 18.130 -19.192 -1.892  1.00 16.26 ?  145 ASP   A CB   1 
ATOM   3131 C  CG   . ASP   A 1 145 ? 16.681 -19.635 -2.028  1.00 18.60 ?  145 ASP   A CG   1 
ATOM   3132 O  OD1  . ASP   A 1 145 ? 16.111 -20.169 -1.050  1.00 18.98 ?  145 ASP   A OD1  1 
ATOM   3133 O  OD2  . ASP   A 1 145 ? 16.111 -19.439 -3.120  1.00 20.14 -1 145 ASP   A OD2  1 
ATOM   3134 H  H    . ASP   A 1 145 ? 17.615 -17.331 -0.361  1.00 16.93 ?  145 ASP   A H    1 
ATOM   3135 H  HA   . ASP   A 1 145 ? 18.334 -19.874 0.026   1.00 17.36 ?  145 ASP   A HA   1 
ATOM   3136 H  HB2  . ASP   A 1 145 ? 18.235 -18.335 -2.335  1.00 19.49 ?  145 ASP   A HB2  1 
ATOM   3137 H  HB3  . ASP   A 1 145 ? 18.686 -19.859 -2.324  1.00 19.49 ?  145 ASP   A HB3  1 
ATOM   3138 N  N    . THR   A 1 146 ? 20.616 -17.816 0.170   1.00 12.82 ?  146 THR   A N    1 
ATOM   3139 C  CA   . THR   A 1 146 ? 22.055 -17.559 0.181   1.00 12.63 ?  146 THR   A CA   1 
ATOM   3140 C  C    . THR   A 1 146 ? 22.610 -17.379 1.581   1.00 12.56 ?  146 THR   A C    1 
ATOM   3141 O  O    . THR   A 1 146 ? 23.690 -17.907 1.893   1.00 13.68 ?  146 THR   A O    1 
ATOM   3142 C  CB   . THR   A 1 146 ? 22.374 -16.306 -0.657  1.00 12.87 ?  146 THR   A CB   1 
ATOM   3143 O  OG1  . THR   A 1 146 ? 21.853 -16.477 -1.976  1.00 13.19 ?  146 THR   A OG1  1 
ATOM   3144 C  CG2  . THR   A 1 146 ? 23.876 -16.073 -0.744  1.00 13.38 ?  146 THR   A CG2  1 
ATOM   3145 H  H    . THR   A 1 146 ? 20.153 -17.191 0.539   1.00 15.36 ?  146 THR   A H    1 
ATOM   3146 H  HA   . THR   A 1 146 ? 22.517 -18.305 -0.223  1.00 15.14 ?  146 THR   A HA   1 
ATOM   3147 H  HB   . THR   A 1 146 ? 21.974 -15.522 -0.242  1.00 15.43 ?  146 THR   A HB   1 
ATOM   3148 H  HG1  . THR   A 1 146 ? 21.018 -16.552 -1.942  1.00 15.82 ?  146 THR   A HG1  1 
ATOM   3149 H  HG21 . THR   A 1 146 ? 24.067 -15.405 -1.420  1.00 16.04 ?  146 THR   A HG21 1 
ATOM   3150 H  HG22 . THR   A 1 146 ? 24.215 -15.761 0.110   1.00 16.04 ?  146 THR   A HG22 1 
ATOM   3151 H  HG23 . THR   A 1 146 ? 24.322 -16.899 -0.981  1.00 16.04 ?  146 THR   A HG23 1 
ATOM   3152 N  N    . VAL   A 1 147 ? 21.931 -16.599 2.414   1.00 12.65 ?  147 VAL   A N    1 
ATOM   3153 C  CA   . VAL   A 1 147 ? 22.416 -16.299 3.752   1.00 12.81 ?  147 VAL   A CA   1 
ATOM   3154 C  C    . VAL   A 1 147 ? 22.095 -17.468 4.670   1.00 13.06 ?  147 VAL   A C    1 
ATOM   3155 O  O    . VAL   A 1 147 ? 20.953 -17.945 4.718   1.00 13.74 ?  147 VAL   A O    1 
ATOM   3156 C  CB   . VAL   A 1 147 ? 21.796 -14.992 4.269   1.00 12.94 ?  147 VAL   A CB   1 
ATOM   3157 C  CG1  . VAL   A 1 147 ? 22.333 -14.674 5.649   1.00 14.16 ?  147 VAL   A CG1  1 
ATOM   3158 C  CG2  . VAL   A 1 147 ? 22.055 -13.852 3.299   1.00 12.90 ?  147 VAL   A CG2  1 
ATOM   3159 H  H    . VAL   A 1 147 ? 21.172 -16.235 2.229   1.00 15.16 ?  147 VAL   A H    1 
ATOM   3160 H  HA   . VAL   A 1 147 ? 23.378 -16.188 3.724   1.00 15.36 ?  147 VAL   A HA   1 
ATOM   3161 H  HB   . VAL   A 1 147 ? 20.837 -15.107 4.346   1.00 15.51 ?  147 VAL   A HB   1 
ATOM   3162 H  HG11 . VAL   A 1 147 ? 22.081 -13.771 5.884   1.00 16.97 ?  147 VAL   A HG11 1 
ATOM   3163 H  HG12 . VAL   A 1 147 ? 21.955 -15.301 6.287   1.00 16.97 ?  147 VAL   A HG12 1 
ATOM   3164 H  HG13 . VAL   A 1 147 ? 23.300 -14.758 5.636   1.00 16.97 ?  147 VAL   A HG13 1 
ATOM   3165 H  HG21 . VAL   A 1 147 ? 21.731 -13.026 3.692   1.00 15.46 ?  147 VAL   A HG21 1 
ATOM   3166 H  HG22 . VAL   A 1 147 ? 23.005 -13.791 3.131   1.00 15.46 ?  147 VAL   A HG22 1 
ATOM   3167 H  HG23 . VAL   A 1 147 ? 21.580 -14.031 2.472   1.00 15.46 ?  147 VAL   A HG23 1 
ATOM   3168 N  N    . ARG   A 1 148 ? 23.112 -17.930 5.395   1.00 13.35 ?  148 ARG   A N    1 
ATOM   3169 C  CA   . ARG   A 1 148 ? 22.980 -19.009 6.358   1.00 13.86 ?  148 ARG   A CA   1 
ATOM   3170 C  C    . ARG   A 1 148 ? 23.106 -18.538 7.795   1.00 13.92 ?  148 ARG   A C    1 
ATOM   3171 O  O    . ARG   A 1 148 ? 22.698 -19.268 8.709   1.00 15.45 ?  148 ARG   A O    1 
ATOM   3172 C  CB   . ARG   A 1 148 ? 24.022 -20.104 6.082   1.00 14.27 ?  148 ARG   A CB   1 
ATOM   3173 C  CG   . ARG   A 1 148 ? 23.864 -20.744 4.713   1.00 15.66 ?  148 ARG   A CG   1 
ATOM   3174 C  CD   . ARG   A 1 148 ? 24.953 -21.780 4.425   1.00 16.45 ?  148 ARG   A CD   1 
ATOM   3175 N  NE   . ARG   A 1 148 ? 26.292 -21.202 4.457   1.00 16.29 ?  148 ARG   A NE   1 
ATOM   3176 C  CZ   . ARG   A 1 148 ? 26.810 -20.465 3.483   1.00 15.47 ?  148 ARG   A CZ   1 
ATOM   3177 N  NH1  . ARG   A 1 148 ? 26.140 -20.227 2.366   1.00 15.98 ?  148 ARG   A NH1  1 
ATOM   3178 N  NH2  . ARG   A 1 148 ? 28.029 -19.946 3.637   1.00 15.82 ?  148 ARG   A NH2  1 
ATOM   3179 H  H    . ARG   A 1 148 ? 23.914 -17.617 5.335   1.00 16.00 ?  148 ARG   A H    1 
ATOM   3180 H  HA   . ARG   A 1 148 ? 22.107 -19.406 6.258   1.00 16.62 ?  148 ARG   A HA   1 
ATOM   3181 H  HB2  . ARG   A 1 148 ? 24.910 -19.726 6.130   1.00 17.11 ?  148 ARG   A HB2  1 
ATOM   3182 H  HB3  . ARG   A 1 148 ? 23.922 -20.809 6.743   1.00 17.11 ?  148 ARG   A HB3  1 
ATOM   3183 H  HG2  . ARG   A 1 148 ? 23.001 -21.181 4.667   1.00 18.77 ?  148 ARG   A HG2  1 
ATOM   3184 H  HG3  . ARG   A 1 148 ? 23.918 -20.046 4.036   1.00 18.77 ?  148 ARG   A HG3  1 
ATOM   3185 H  HD2  . ARG   A 1 148 ? 24.908 -22.475 5.096   1.00 19.73 ?  148 ARG   A HD2  1 
ATOM   3186 H  HD3  . ARG   A 1 148 ? 24.803 -22.154 3.542   1.00 19.73 ?  148 ARG   A HD3  1 
ATOM   3187 H  HE   . ARG   A 1 148 ? 26.773 -21.343 5.151   1.00 19.53 ?  148 ARG   A HE   1 
ATOM   3188 H  HH11 . ARG   A 1 148 ? 25.349 -20.542 2.255   1.00 19.16 ?  148 ARG   A HH11 1 
ATOM   3189 H  HH12 . ARG   A 1 148 ? 26.493 -19.735 1.749   1.00 19.16 ?  148 ARG   A HH12 1 
ATOM   3190 H  HH21 . ARG   A 1 148 ? 28.468 -20.088 4.360   1.00 18.97 ?  148 ARG   A HH21 1 
ATOM   3191 H  HH22 . ARG   A 1 148 ? 28.372 -19.460 3.013   1.00 18.97 ?  148 ARG   A HH22 1 
ATOM   3192 N  N    . THR   A 1 149 ? 23.650 -17.340 8.007   1.00 13.91 ?  149 THR   A N    1 
ATOM   3193 C  CA   . THR   A 1 149 ? 23.724 -16.741 9.324   1.00 14.02 ?  149 THR   A CA   1 
ATOM   3194 C  C    . THR   A 1 149 ? 22.398 -16.045 9.626   1.00 13.54 ?  149 THR   A C    1 
ATOM   3195 O  O    . THR   A 1 149 ? 21.466 -16.040 8.811   1.00 14.22 ?  149 THR   A O    1 
ATOM   3196 C  CB   . THR   A 1 149 ? 24.924 -15.801 9.388   1.00 14.69 ?  149 THR   A CB   1 
ATOM   3197 O  OG1  . THR   A 1 149 ? 24.807 -14.874 8.307   1.00 14.63 ?  149 THR   A OG1  1 
ATOM   3198 C  CG2  . THR   A 1 149 ? 26.235 -16.594 9.280   1.00 15.43 ?  149 THR   A CG2  1 
ATOM   3199 H  H    . THR   A 1 149 ? 23.990 -16.846 7.385   1.00 16.68 ?  149 THR   A H    1 
ATOM   3200 H  HA   . THR   A 1 149 ? 23.849 -17.443 9.980   1.00 16.81 ?  149 THR   A HA   1 
ATOM   3201 H  HB   . THR   A 1 149 ? 24.907 -15.325 10.230  1.00 17.61 ?  149 THR   A HB   1 
ATOM   3202 H  HG1  . THR   A 1 149 ? 25.455 -14.341 8.315   1.00 17.54 ?  149 THR   A HG1  1 
ATOM   3203 H  HG21 . THR   A 1 149 ? 26.992 -15.992 9.334   1.00 18.50 ?  149 THR   A HG21 1 
ATOM   3204 H  HG22 . THR   A 1 149 ? 26.295 -17.243 10.001  1.00 18.50 ?  149 THR   A HG22 1 
ATOM   3205 H  HG23 . THR   A 1 149 ? 26.271 -17.069 8.432   1.00 18.50 ?  149 THR   A HG23 1 
ATOM   3206 N  N    . ASN   A 1 150 ? 22.276 -15.503 10.831  1.00 13.75 ?  150 ASN   A N    1 
ATOM   3207 C  CA   . ASN   A 1 150 ? 20.994 -14.986 11.311  1.00 14.29 ?  150 ASN   A CA   1 
ATOM   3208 C  C    . ASN   A 1 150 ? 20.818 -13.548 10.845  1.00 13.31 ?  150 ASN   A C    1 
ATOM   3209 O  O    . ASN   A 1 150 ? 21.568 -12.652 11.257  1.00 14.70 ?  150 ASN   A O    1 
ATOM   3210 C  CB   . ASN   A 1 150 ? 20.929 -15.094 12.829  1.00 17.01 ?  150 ASN   A CB   1 
ATOM   3211 C  CG   . ASN   A 1 150 ? 20.833 -16.526 13.295  1.00 20.94 ?  150 ASN   A CG   1 
ATOM   3212 O  OD1  . ASN   A 1 150 ? 20.229 -17.360 12.622  1.00 22.13 ?  150 ASN   A OD1  1 
ATOM   3213 N  ND2  . ASN   A 1 150 ? 21.436 -16.826 14.443  1.00 23.37 ?  150 ASN   A ND2  1 
ATOM   3214 H  H    . ASN   A 1 150 ? 22.915 -15.431 11.399  1.00 16.48 ?  150 ASN   A H    1 
ATOM   3215 H  HA   . ASN   A 1 150 ? 20.269 -15.522 10.942  1.00 17.13 ?  150 ASN   A HA   1 
ATOM   3216 H  HB2  . ASN   A 1 150 ? 21.730 -14.709 13.213  1.00 20.40 ?  150 ASN   A HB2  1 
ATOM   3217 H  HB3  . ASN   A 1 150 ? 20.143 -14.626 13.153  1.00 20.40 ?  150 ASN   A HB3  1 
ATOM   3218 H  HD21 . ASN   A 1 150 ? 21.413 -17.632 14.751  1.00 28.02 ?  150 ASN   A HD21 1 
ATOM   3219 H  HD22 . ASN   A 1 150 ? 21.849 -16.214 14.886  1.00 28.02 ?  150 ASN   A HD22 1 
ATOM   3220 N  N    . VAL   A 1 151 ? 19.825 -13.320 9.991   1.00 12.92 ?  151 VAL   A N    1 
ATOM   3221 C  CA   . VAL   A 1 151 ? 19.611 -12.016 9.380   1.00 13.03 ?  151 VAL   A CA   1 
ATOM   3222 C  C    . VAL   A 1 151 ? 18.222 -11.500 9.738   1.00 12.84 ?  151 VAL   A C    1 
ATOM   3223 O  O    . VAL   A 1 151 ? 17.215 -12.212 9.594   1.00 14.18 ?  151 VAL   A O    1 
ATOM   3224 C  CB   . VAL   A 1 151 ? 19.895 -12.025 7.862   1.00 14.21 ?  151 VAL   A CB   1 
ATOM   3225 C  CG1  . VAL   A 1 151 ? 19.072 -13.063 7.133   1.00 15.41 ?  151 VAL   A CG1  1 
ATOM   3226 C  CG2  . VAL   A 1 151 ? 19.695 -10.629 7.268   1.00 14.34 ?  151 VAL   A CG2  1 
ATOM   3227 H  H    . VAL   A 1 151 ? 19.253 -13.916 9.747   1.00 15.49 ?  151 VAL   A H    1 
ATOM   3228 H  HA   . VAL   A 1 151 ? 20.257 -11.401 9.768   1.00 15.62 ?  151 VAL   A HA   1 
ATOM   3229 H  HB   . VAL   A 1 151 ? 20.829 -12.257 7.724   1.00 17.04 ?  151 VAL   A HB   1 
ATOM   3230 H  HG11 . VAL   A 1 151 ? 19.263 -13.021 6.181   1.00 18.48 ?  151 VAL   A HG11 1 
ATOM   3231 H  HG12 . VAL   A 1 151 ? 19.300 -13.948 7.470   1.00 18.48 ?  151 VAL   A HG12 1 
ATOM   3232 H  HG13 . VAL   A 1 151 ? 18.128 -12.892 7.285   1.00 18.48 ?  151 VAL   A HG13 1 
ATOM   3233 H  HG21 . VAL   A 1 151 ? 20.011 -10.629 6.347   1.00 17.20 ?  151 VAL   A HG21 1 
ATOM   3234 H  HG22 . VAL   A 1 151 ? 18.751 -10.407 7.288   1.00 17.20 ?  151 VAL   A HG22 1 
ATOM   3235 H  HG23 . VAL   A 1 151 ? 20.200 -9.987  7.787   1.00 17.20 ?  151 VAL   A HG23 1 
ATOM   3236 N  N    . TYR   A 1 152 ? 18.202 -10.255 10.219  1.00 12.91 ?  152 TYR   A N    1 
ATOM   3237 C  CA   . TYR   A 1 152 ? 17.008 -9.525  10.604  1.00 12.59 ?  152 TYR   A CA   1 
ATOM   3238 C  C    . TYR   A 1 152 ? 16.813 -8.424  9.577   1.00 12.06 ?  152 TYR   A C    1 
ATOM   3239 O  O    . TYR   A 1 152 ? 17.590 -7.462  9.535   1.00 12.48 ?  152 TYR   A O    1 
ATOM   3240 C  CB   . TYR   A 1 152 ? 17.184 -8.981  12.018  1.00 13.44 ?  152 TYR   A CB   1 
ATOM   3241 C  CG   . TYR   A 1 152 ? 17.136 -10.101 13.015  1.00 14.16 ?  152 TYR   A CG   1 
ATOM   3242 C  CD1  . TYR   A 1 152 ? 18.263 -10.866 13.292  1.00 15.68 ?  152 TYR   A CD1  1 
ATOM   3243 C  CD2  . TYR   A 1 152 ? 15.948 -10.443 13.638  1.00 14.40 ?  152 TYR   A CD2  1 
ATOM   3244 C  CE1  . TYR   A 1 152 ? 18.215 -11.923 14.178  1.00 17.24 ?  152 TYR   A CE1  1 
ATOM   3245 C  CE2  . TYR   A 1 152 ? 15.887 -11.504 14.530  1.00 16.33 ?  152 TYR   A CE2  1 
ATOM   3246 C  CZ   . TYR   A 1 152 ? 17.026 -12.239 14.798  1.00 17.33 ?  152 TYR   A CZ   1 
ATOM   3247 O  OH   . TYR   A 1 152 ? 16.974 -13.301 15.679  1.00 19.76 ?  152 TYR   A OH   1 
ATOM   3248 H  H    . TYR   A 1 152 ? 18.927 -9.782  10.322  1.00 15.47 ?  152 TYR   A H    1 
ATOM   3249 H  HA   . TYR   A 1 152 ? 16.247 -10.121 10.585  1.00 15.09 ?  152 TYR   A HA   1 
ATOM   3250 H  HB2  . TYR   A 1 152 ? 18.048 -8.545  12.091  1.00 16.12 ?  152 TYR   A HB2  1 
ATOM   3251 H  HB3  . TYR   A 1 152 ? 16.471 -8.361  12.216  1.00 16.12 ?  152 TYR   A HB3  1 
ATOM   3252 H  HD1  . TYR   A 1 152 ? 19.066 -10.659 12.870  1.00 18.80 ?  152 TYR   A HD1  1 
ATOM   3253 H  HD2  . TYR   A 1 152 ? 15.177 -9.950  13.456  1.00 17.26 ?  152 TYR   A HD2  1 
ATOM   3254 H  HE1  . TYR   A 1 152 ? 18.979 -12.417 14.358  1.00 20.67 ?  152 TYR   A HE1  1 
ATOM   3255 H  HE2  . TYR   A 1 152 ? 15.082 -11.712 14.948  1.00 19.58 ?  152 TYR   A HE2  1 
ATOM   3256 H  HH   . TYR   A 1 152 ? 16.197 -13.371 15.992  1.00 23.70 ?  152 TYR   A HH   1 
ATOM   3257 N  N    . LEU   A 1 153 ? 15.799 -8.582  8.734   1.00 12.31 ?  153 LEU   A N    1 
ATOM   3258 C  CA   . LEU   A 1 153 ? 15.543 -7.684  7.616   1.00 12.33 ?  153 LEU   A CA   1 
ATOM   3259 C  C    . LEU   A 1 153 ? 14.547 -6.606  8.015   1.00 12.64 ?  153 LEU   A C    1 
ATOM   3260 O  O    . LEU   A 1 153 ? 13.438 -6.908  8.479   1.00 13.84 ?  153 LEU   A O    1 
ATOM   3261 C  CB   . LEU   A 1 153 ? 14.978 -8.462  6.428   1.00 12.42 ?  153 LEU   A CB   1 
ATOM   3262 C  CG   . LEU   A 1 153 ? 15.923 -9.479  5.781   1.00 12.59 ?  153 LEU   A CG   1 
ATOM   3263 C  CD1  . LEU   A 1 153 ? 15.144 -10.374 4.830   1.00 13.26 ?  153 LEU   A CD1  1 
ATOM   3264 C  CD2  . LEU   A 1 153 ? 17.059 -8.781  5.047   1.00 12.98 ?  153 LEU   A CD2  1 
ATOM   3265 H  H    . LEU   A 1 153 ? 15.221 -9.225  8.800   1.00 14.75 ?  153 LEU   A H    1 
ATOM   3266 H  HA   . LEU   A 1 153 ? 16.370 -7.265  7.355   1.00 14.78 ?  153 LEU   A HA   1 
ATOM   3267 H  HB2  . LEU   A 1 153 ? 14.192 -8.944  6.726   1.00 14.89 ?  153 LEU   A HB2  1 
ATOM   3268 H  HB3  . LEU   A 1 153 ? 14.728 -7.823  5.744   1.00 14.89 ?  153 LEU   A HB3  1 
ATOM   3269 H  HG   . LEU   A 1 153 ? 16.312 -10.034 6.479   1.00 15.10 ?  153 LEU   A HG   1 
ATOM   3270 H  HD11 . LEU   A 1 153 ? 15.732 -11.070 4.507   1.00 15.89 ?  153 LEU   A HD11 1 
ATOM   3271 H  HD12 . LEU   A 1 153 ? 14.397 -10.760 5.308   1.00 15.89 ?  153 LEU   A HD12 1 
ATOM   3272 H  HD13 . LEU   A 1 153 ? 14.825 -9.834  4.091   1.00 15.89 ?  153 LEU   A HD13 1 
ATOM   3273 H  HD21 . LEU   A 1 153 ? 17.632 -9.454  4.655   1.00 15.56 ?  153 LEU   A HD21 1 
ATOM   3274 H  HD22 . LEU   A 1 153 ? 16.678 -8.220  4.355   1.00 15.56 ?  153 LEU   A HD22 1 
ATOM   3275 H  HD23 . LEU   A 1 153 ? 17.558 -8.243  5.679   1.00 15.56 ?  153 LEU   A HD23 1 
ATOM   3276 N  N    A ALA   A 1 154 ? 14.924 -5.355  7.779   0.70 12.41 ?  154 ALA   A N    1 
ATOM   3277 N  N    B ALA   A 1 154 ? 14.956 -5.350  7.857   0.30 12.19 ?  154 ALA   A N    1 
ATOM   3278 C  CA   A ALA   A 1 154 ? 14.040 -4.212  7.957   0.70 12.67 ?  154 ALA   A CA   1 
ATOM   3279 C  CA   B ALA   A 1 154 ? 14.136 -4.192  8.182   0.30 12.22 ?  154 ALA   A CA   1 
ATOM   3280 C  C    A ALA   A 1 154 ? 13.570 -3.741  6.585   0.70 12.20 ?  154 ALA   A C    1 
ATOM   3281 C  C    B ALA   A 1 154 ? 13.602 -3.609  6.881   0.30 12.00 ?  154 ALA   A C    1 
ATOM   3282 O  O    A ALA   A 1 154 ? 14.390 -3.399  5.726   0.70 13.10 ?  154 ALA   A O    1 
ATOM   3283 O  O    B ALA   A 1 154 ? 14.377 -3.127  6.049   0.30 12.07 ?  154 ALA   A O    1 
ATOM   3284 C  CB   A ALA   A 1 154 ? 14.782 -3.086  8.672   0.70 13.31 ?  154 ALA   A CB   1 
ATOM   3285 C  CB   B ALA   A 1 154 ? 14.960 -3.147  8.934   0.30 12.42 ?  154 ALA   A CB   1 
ATOM   3286 H  H    A ALA   A 1 154 ? 15.711 -5.140  7.503   0.70 14.88 ?  154 ALA   A H    1 
ATOM   3287 H  H    B ALA   A 1 154 ? 15.729 -5.138  7.541   0.30 14.61 ?  154 ALA   A H    1 
ATOM   3288 H  HA   A ALA   A 1 154 ? 13.269 -4.471  8.487   0.70 15.19 ?  154 ALA   A HA   1 
ATOM   3289 H  HA   B ALA   A 1 154 ? 13.386 -4.457  8.737   0.30 14.65 ?  154 ALA   A HA   1 
ATOM   3290 H  HB1  A ALA   A 1 154 ? 14.180 -2.334  8.781   0.70 15.96 ?  154 ALA   A HB1  1 
ATOM   3291 H  HB1  B ALA   A 1 154 ? 14.396 -2.384  9.140   0.30 14.89 ?  154 ALA   A HB1  1 
ATOM   3292 H  HB2  A ALA   A 1 154 ? 15.078 -3.404  9.539   0.70 15.96 ?  154 ALA   A HB2  1 
ATOM   3293 H  HB2  B ALA   A 1 154 ? 15.297 -3.540  9.754   0.30 14.89 ?  154 ALA   A HB2  1 
ATOM   3294 H  HB3  A ALA   A 1 154 ? 15.547 -2.824  8.135   0.70 15.96 ?  154 ALA   A HB3  1 
ATOM   3295 H  HB3  B ALA   A 1 154 ? 15.702 -2.865  8.373   0.30 14.89 ?  154 ALA   A HB3  1 
ATOM   3296 N  N    A VAL   A 1 155 ? 12.255 -3.736  6.386   0.40 10.39 ?  155 VAL   A N    1 
ATOM   3297 N  N    B VAL   A 1 155 ? 12.285 -3.660  6.708   0.30 11.62 ?  155 VAL   A N    1 
ATOM   3298 C  CA   A VAL   A 1 155 ? 11.617 -3.278  5.155   0.40 12.33 ?  155 VAL   A CA   1 
ATOM   3299 C  CA   B VAL   A 1 155 ? 11.619 -3.203  5.494   0.30 12.70 ?  155 VAL   A CA   1 
ATOM   3300 C  CA   T VAL   A 1 155 ? 11.607 -3.333  5.185   0.30 14.17 ?  155 VAL   A CA   1 
ATOM   3301 C  C    A VAL   A 1 155 ? 10.871 -1.990  5.490   0.40 13.65 ?  155 VAL   A C    1 
ATOM   3302 C  C    B VAL   A 1 155 ? 10.987 -1.847  5.778   0.30 14.04 ?  155 VAL   A C    1 
ATOM   3303 C  C    T VAL   A 1 155 ? 10.971 -1.972  5.480   0.30 14.05 ?  155 VAL   A C    1 
ATOM   3304 O  O    A VAL   A 1 155 ? 9.865  -2.020  6.209   0.40 13.63 ?  155 VAL   A O    1 
ATOM   3305 O  O    B VAL   A 1 155 ? 10.188 -1.707  6.711   0.30 13.72 ?  155 VAL   A O    1 
ATOM   3306 O  O    T VAL   A 1 155 ? 10.083 -1.862  6.325   0.30 13.70 ?  155 VAL   A O    1 
ATOM   3307 C  CB   A VAL   A 1 155 ? 10.674 -4.348  4.583   0.40 12.54 ?  155 VAL   A CB   1 
ATOM   3308 C  CB   B VAL   A 1 155 ? 10.576 -4.224  5.015   0.30 12.72 ?  155 VAL   A CB   1 
ATOM   3309 C  CB   T VAL   A 1 155 ? 10.591 -4.365  4.660   0.30 14.14 ?  155 VAL   A CB   1 
ATOM   3310 C  CG1  A VAL   A 1 155 ? 9.984  -3.848  3.321   0.40 13.08 ?  155 VAL   A CG1  1 
ATOM   3311 C  CG1  B VAL   A 1 155 ? 9.829  -3.697  3.799   0.30 13.04 ?  155 VAL   A CG1  1 
ATOM   3312 C  CG1  T VAL   A 1 155 ? 9.890  -3.840  3.420   0.30 14.46 ?  155 VAL   A CG1  1 
ATOM   3313 C  CG2  A VAL   A 1 155 ? 11.444 -5.636  4.301   0.40 13.47 ?  155 VAL   A CG2  1 
ATOM   3314 C  CG2  B VAL   A 1 155 ? 11.249 -5.551  4.700   0.30 12.89 ?  155 VAL   A CG2  1 
ATOM   3315 C  CG2  T VAL   A 1 155 ? 11.285 -5.692  4.361   0.30 14.54 ?  155 VAL   A CG2  1 
ATOM   3316 H  H    A VAL   A 1 155 ? 11.686 -4.017  6.972   0.40 12.45 ?  155 VAL   A H    1 
ATOM   3317 H  H    B VAL   A 1 155 ? 11.740 -3.960  7.298   0.30 13.92 ?  155 VAL   A H    1 
ATOM   3318 H  HA   A VAL   A 1 155 ? 12.296 -3.081  4.493   0.40 14.78 ?  155 VAL   A HA   1 
ATOM   3319 H  HA   B VAL   A 1 155 ? 12.275 -3.090  4.788   0.30 15.22 ?  155 VAL   A HA   1 
ATOM   3320 H  HB   A VAL   A 1 155 ? 9.989  -4.550  5.239   0.40 15.03 ?  155 VAL   A HB   1 
ATOM   3321 H  HB   B VAL   A 1 155 ? 9.931  -4.376  5.724   0.30 15.24 ?  155 VAL   A HB   1 
ATOM   3322 H  HB   T VAL   A 1 155 ? 9.924  -4.524  5.345   0.30 16.96 ?  155 VAL   A HB   1 
ATOM   3323 H  HG11 A VAL   A 1 155 ? 9.516  -4.589  2.904   0.40 15.67 ?  155 VAL   A HG11 1 
ATOM   3324 H  HG11 B VAL   A 1 155 ? 9.308  -4.418  3.412   0.30 15.63 ?  155 VAL   A HG11 1 
ATOM   3325 H  HG11 T VAL   A 1 155 ? 9.373  -4.559  3.025   0.30 17.33 ?  155 VAL   A HG11 1 
ATOM   3326 H  HG12 A VAL   A 1 155 ? 9.351  -3.153  3.561   0.40 15.67 ?  155 VAL   A HG12 1 
ATOM   3327 H  HG12 B VAL   A 1 155 ? 9.240  -2.978  4.074   0.30 15.63 ?  155 VAL   A HG12 1 
ATOM   3328 H  HG12 T VAL   A 1 155 ? 9.304  -3.111  3.674   0.30 17.33 ?  155 VAL   A HG12 1 
ATOM   3329 H  HG13 A VAL   A 1 155 ? 10.652 -3.496  2.715   0.40 15.67 ?  155 VAL   A HG13 1 
ATOM   3330 H  HG13 B VAL   A 1 155 ? 10.473 -3.370  3.151   0.30 15.63 ?  155 VAL   A HG13 1 
ATOM   3331 H  HG13 T VAL   A 1 155 ? 10.558 -3.528  2.789   0.30 17.33 ?  155 VAL   A HG13 1 
ATOM   3332 H  HG21 A VAL   A 1 155 ? 10.848 -6.277  3.883   0.40 16.15 ?  155 VAL   A HG21 1 
ATOM   3333 H  HG21 B VAL   A 1 155 ? 10.649 -6.091  4.165   0.30 15.45 ?  155 VAL   A HG21 1 
ATOM   3334 H  HG21 T VAL   A 1 155 ? 10.628 -6.327  4.037   0.30 17.43 ?  155 VAL   A HG21 1 
ATOM   3335 H  HG22 A VAL   A 1 155 ? 12.185 -5.438  3.706   0.40 16.15 ?  155 VAL   A HG22 1 
ATOM   3336 H  HG22 B VAL   A 1 155 ? 12.067 -5.378  4.203   0.30 15.45 ?  155 VAL   A HG22 1 
ATOM   3337 H  HG22 T VAL   A 1 155 ? 11.966 -5.547  3.683   0.30 17.43 ?  155 VAL   A HG22 1 
ATOM   3338 H  HG23 A VAL   A 1 155 ? 11.780 -5.994  5.138   0.40 16.15 ?  155 VAL   A HG23 1 
ATOM   3339 H  HG23 B VAL   A 1 155 ? 11.461 -6.005  5.530   0.30 15.45 ?  155 VAL   A HG23 1 
ATOM   3340 H  HG23 T VAL   A 1 155 ? 11.697 -6.026  5.174   0.30 17.43 ?  155 VAL   A HG23 1 
ATOM   3341 N  N    A PHE   A 1 156 ? 11.368 -0.855  4.983   0.40 15.25 ?  156 PHE   A N    1 
ATOM   3342 N  N    B PHE   A 1 156 ? 11.339 -0.852  4.961   0.30 15.47 ?  156 PHE   A N    1 
ATOM   3343 N  N    T PHE   A 1 156 ? 11.443 -0.942  4.773   0.30 14.48 ?  156 PHE   A N    1 
ATOM   3344 C  CA   A PHE   A 1 156 ? 10.803 0.446   5.353   0.40 16.78 ?  156 PHE   A CA   1 
ATOM   3345 C  CA   B PHE   A 1 156 ? 10.926 0.523   5.227   0.30 16.79 ?  156 PHE   A CA   1 
ATOM   3346 C  CA   T PHE   A 1 156 ? 11.024 0.428   5.064   0.30 15.04 ?  156 PHE   A CA   1 
ATOM   3347 C  C    A PHE   A 1 156 ? 9.348  0.589   4.913   0.40 16.83 ?  156 PHE   A C    1 
ATOM   3348 C  C    B PHE   A 1 156 ? 9.422  0.702   5.034   0.30 18.00 ?  156 PHE   A C    1 
ATOM   3349 C  C    T PHE   A 1 156 ? 9.567  0.664   4.682   0.30 15.38 ?  156 PHE   A C    1 
ATOM   3350 O  O    A PHE   A 1 156 ? 8.512  1.101   5.669   0.40 17.47 ?  156 PHE   A O    1 
ATOM   3351 O  O    B PHE   A 1 156 ? 8.738  1.267   5.896   0.30 18.19 ?  156 PHE   A O    1 
ATOM   3352 O  O    T PHE   A 1 156 ? 8.832  1.350   5.403   0.30 15.74 ?  156 PHE   A O    1 
ATOM   3353 C  CB   A PHE   A 1 156 ? 11.663 1.571   4.766   0.40 17.93 ?  156 PHE   A CB   1 
ATOM   3354 C  CB   B PHE   A 1 156 ? 11.712 1.465   4.311   0.30 16.51 ?  156 PHE   A CB   1 
ATOM   3355 C  CB   T PHE   A 1 156 ? 11.934 1.401   4.312   0.30 14.58 ?  156 PHE   A CB   1 
ATOM   3356 C  CG   A PHE   A 1 156 ? 11.156 2.959   5.080   0.40 19.09 ?  156 PHE   A CG   1 
ATOM   3357 C  CG   B PHE   A 1 156 ? 11.464 2.926   4.577   0.30 16.45 ?  156 PHE   A CG   1 
ATOM   3358 C  CG   T PHE   A 1 156 ? 11.579 2.856   4.506   0.30 14.43 ?  156 PHE   A CG   1 
ATOM   3359 C  CD1  A PHE   A 1 156 ? 11.068 3.395   6.391   0.40 19.53 ?  156 PHE   A CD1  1 
ATOM   3360 C  CD1  B PHE   A 1 156 ? 12.184 3.597   5.555   0.30 16.51 ?  156 PHE   A CD1  1 
ATOM   3361 C  CD1  T PHE   A 1 156 ? 11.927 3.520   5.674   0.30 15.32 ?  156 PHE   A CD1  1 
ATOM   3362 C  CD2  A PHE   A 1 156 ? 10.790 3.830   4.064   0.40 19.91 ?  156 PHE   A CD2  1 
ATOM   3363 C  CD2  B PHE   A 1 156 ? 10.527 3.631   3.841   0.30 17.22 ?  156 PHE   A CD2  1 
ATOM   3364 C  CD2  T PHE   A 1 156 ? 10.919 3.564   3.512   0.30 14.36 ?  156 PHE   A CD2  1 
ATOM   3365 C  CE1  A PHE   A 1 156 ? 10.611 4.667   6.688   0.40 20.13 ?  156 PHE   A CE1  1 
ATOM   3366 C  CE1  B PHE   A 1 156 ? 11.965 4.939   5.804   0.30 16.82 ?  156 PHE   A CE1  1 
ATOM   3367 C  CE1  T PHE   A 1 156 ? 11.610 4.853   5.855   0.30 15.81 ?  156 PHE   A CE1  1 
ATOM   3368 C  CE2  A PHE   A 1 156 ? 10.330 5.106   4.354   0.40 20.71 ?  156 PHE   A CE2  1 
ATOM   3369 C  CE2  B PHE   A 1 156 ? 10.300 4.974   4.085   0.30 17.74 ?  156 PHE   A CE2  1 
ATOM   3370 C  CE2  T PHE   A 1 156 ? 10.602 4.900   3.685   0.30 15.07 ?  156 PHE   A CE2  1 
ATOM   3371 C  CZ   A PHE   A 1 156 ? 10.244 5.524   5.668   0.40 20.68 ?  156 PHE   A CZ   1 
ATOM   3372 C  CZ   B PHE   A 1 156 ? 11.025 5.631   5.067   0.30 17.28 ?  156 PHE   A CZ   1 
ATOM   3373 C  CZ   T PHE   A 1 156 ? 10.949 5.546   4.859   0.30 15.63 ?  156 PHE   A CZ   1 
ATOM   3374 H  H    A PHE   A 1 156 ? 12.040 -0.815  4.445   0.40 18.29 ?  156 PHE   A H    1 
ATOM   3375 H  H    B PHE   A 1 156 ? 11.811 -0.952  4.249   0.30 18.54 ?  156 PHE   A H    1 
ATOM   3376 H  H    T PHE   A 1 156 ? 12.006 -1.013  4.127   0.30 17.36 ?  156 PHE   A H    1 
ATOM   3377 H  HA   A PHE   A 1 156 ? 10.830 0.535   6.316   0.40 20.12 ?  156 PHE   A HA   1 
ATOM   3378 H  HA   B PHE   A 1 156 ? 11.148 0.745   6.146   0.30 20.13 ?  156 PHE   A HA   1 
ATOM   3379 H  HA   T PHE   A 1 156 ? 11.122 0.593   6.015   0.30 18.04 ?  156 PHE   A HA   1 
ATOM   3380 H  HB2  A PHE   A 1 156 ? 12.565 1.498   5.124   0.40 21.50 ?  156 PHE   A HB2  1 
ATOM   3381 H  HB2  B PHE   A 1 156 ? 12.663 1.299   4.433   0.30 19.80 ?  156 PHE   A HB2  1 
ATOM   3382 H  HB2  T PHE   A 1 156 ? 12.845 1.274   4.620   0.30 17.48 ?  156 PHE   A HB2  1 
ATOM   3383 H  HB3  A PHE   A 1 156 ? 11.688 1.478   3.801   0.40 21.50 ?  156 PHE   A HB3  1 
ATOM   3384 H  HB3  B PHE   A 1 156 ? 11.467 1.283   3.392   0.30 19.80 ?  156 PHE   A HB3  1 
ATOM   3385 H  HB3  T PHE   A 1 156 ? 11.878 1.207   3.364   0.30 17.48 ?  156 PHE   A HB3  1 
ATOM   3386 H  HD1  A PHE   A 1 156 ? 11.317 2.821   7.083   0.40 23.42 ?  156 PHE   A HD1  1 
ATOM   3387 H  HD1  B PHE   A 1 156 ? 12.817 3.130   6.057   0.30 19.79 ?  156 PHE   A HD1  1 
ATOM   3388 H  HD1  T PHE   A 1 156 ? 12.370 3.054   6.351   0.30 18.37 ?  156 PHE   A HD1  1 
ATOM   3389 H  HD2  A PHE   A 1 156 ? 10.850 3.551   3.179   0.40 23.87 ?  156 PHE   A HD2  1 
ATOM   3390 H  HD2  B PHE   A 1 156 ? 10.040 3.193   3.181   0.30 20.65 ?  156 PHE   A HD2  1 
ATOM   3391 H  HD2  T PHE   A 1 156 ? 10.682 3.133   2.725   0.30 17.22 ?  156 PHE   A HD2  1 
ATOM   3392 H  HE1  A PHE   A 1 156 ? 10.556 4.945   7.575   0.40 24.15 ?  156 PHE   A HE1  1 
ATOM   3393 H  HE1  B PHE   A 1 156 ? 12.450 5.372   6.468   0.30 20.17 ?  156 PHE   A HE1  1 
ATOM   3394 H  HE1  T PHE   A 1 156 ? 11.843 5.282   6.649   0.30 18.95 ?  156 PHE   A HE1  1 
ATOM   3395 H  HE2  A PHE   A 1 156 ? 10.087 5.679   3.666   0.40 24.83 ?  156 PHE   A HE2  1 
ATOM   3396 H  HE2  B PHE   A 1 156 ? 9.668  5.437   3.588   0.30 21.27 ?  156 PHE   A HE2  1 
ATOM   3397 H  HE2  T PHE   A 1 156 ? 10.153 5.362   3.018   0.30 18.07 ?  156 PHE   A HE2  1 
ATOM   3398 H  HZ   A PHE   A 1 156 ? 9.938  6.379   5.868   0.40 24.80 ?  156 PHE   A HZ   1 
ATOM   3399 H  HZ   B PHE   A 1 156 ? 10.874 6.532   5.235   0.30 20.72 ?  156 PHE   A HZ   1 
ATOM   3400 H  HZ   T PHE   A 1 156 ? 10.733 6.441   4.983   0.30 18.74 ?  156 PHE   A HZ   1 
ATOM   3401 N  N    A ASP   A 1 157 ? 9.027  0.156   3.697   0.40 16.84 ?  157 ASP   A N    1 
ATOM   3402 N  N    B ASP   A 1 157 ? 8.892  0.220   3.915   0.30 18.93 ?  157 ASP   A N    1 
ATOM   3403 N  N    T ASP   A 1 157 ? 9.134  0.108   3.557   0.30 15.52 ?  157 ASP   A N    1 
ATOM   3404 C  CA   A ASP   A 1 157 ? 7.702  0.391   3.129   0.40 17.75 ?  157 ASP   A CA   1 
ATOM   3405 C  CA   B ASP   A 1 157 ? 7.507  0.460   3.530   0.30 20.28 ?  157 ASP   A CA   1 
ATOM   3406 C  CA   T ASP   A 1 157 ? 7.829  0.409   2.987   0.30 16.11 ?  157 ASP   A CA   1 
ATOM   3407 C  C    A ASP   A 1 157 ? 6.712  -0.628  3.689   0.40 17.89 ?  157 ASP   A C    1 
ATOM   3408 C  C    B ASP   A 1 157 ? 6.590  -0.667  4.009   0.30 20.45 ?  157 ASP   A C    1 
ATOM   3409 C  C    T ASP   A 1 157 ? 6.789  -0.568  3.528   0.30 16.98 ?  157 ASP   A C    1 
ATOM   3410 O  O    A ASP   A 1 157 ? 6.839  -1.830  3.431   0.40 16.78 ?  157 ASP   A O    1 
ATOM   3411 O  O    B ASP   A 1 157 ? 7.016  -1.803  4.228   0.30 20.76 ?  157 ASP   A O    1 
ATOM   3412 O  O    T ASP   A 1 157 ? 6.869  -1.774  3.267   0.30 16.39 ?  157 ASP   A O    1 
ATOM   3413 C  CB   A ASP   A 1 157 ? 7.777  0.300   1.609   0.40 18.49 ?  157 ASP   A CB   1 
ATOM   3414 C  CB   B ASP   A 1 157 ? 7.406  0.601   2.010   0.30 21.44 ?  157 ASP   A CB   1 
ATOM   3415 C  CB   T ASP   A 1 157 ? 7.926  0.316   1.468   0.30 16.02 ?  157 ASP   A CB   1 
ATOM   3416 C  CG   A ASP   A 1 157 ? 6.529  0.819   0.933   0.40 19.51 ?  157 ASP   A CG   1 
ATOM   3417 C  CG   B ASP   A 1 157 ? 6.037  1.074   1.558   0.30 22.62 ?  157 ASP   A CG   1 
ATOM   3418 C  CG   T ASP   A 1 157 ? 6.740  0.909   0.775   0.30 15.80 ?  157 ASP   A CG   1 
ATOM   3419 O  OD1  A ASP   A 1 157 ? 6.281  2.039   1.000   0.40 20.78 ?  157 ASP   A OD1  1 
ATOM   3420 O  OD1  B ASP   A 1 157 ? 5.046  0.369   1.833   0.30 22.94 ?  157 ASP   A OD1  1 
ATOM   3421 O  OD1  T ASP   A 1 157 ? 5.646  0.322   0.892   0.30 15.53 ?  157 ASP   A OD1  1 
ATOM   3422 O  OD2  A ASP   A 1 157 ? 5.793  0.004   0.335   0.40 19.06 -1 157 ASP   A OD2  1 
ATOM   3423 O  OD2  B ASP   A 1 157 ? 5.949  2.154   0.937   0.30 23.31 -1 157 ASP   A OD2  1 
ATOM   3424 O  OD2  T ASP   A 1 157 ? 6.900  1.961   0.125   0.30 15.32 -1 157 ASP   A OD2  1 
ATOM   3425 H  H    A ASP   A 1 157 ? 9.565  -0.282  3.176   0.40 20.19 ?  157 ASP   A H    1 
ATOM   3426 H  H    B ASP   A 1 157 ? 9.331  -0.254  3.352   0.30 22.70 ?  157 ASP   A H    1 
ATOM   3427 H  H    T ASP   A 1 157 ? 9.592  -0.457  3.094   0.30 18.61 ?  157 ASP   A H    1 
ATOM   3428 H  HA   A ASP   A 1 157 ? 7.406  1.277   3.374   0.40 21.29 ?  157 ASP   A HA   1 
ATOM   3429 H  HA   B ASP   A 1 157 ? 7.206  1.290   3.933   0.30 24.32 ?  157 ASP   A HA   1 
ATOM   3430 H  HA   T ASP   A 1 157 ? 7.567  1.307   3.234   0.30 19.32 ?  157 ASP   A HA   1 
ATOM   3431 H  HB2  A ASP   A 1 157 ? 8.552  0.799   1.303   0.40 22.17 ?  157 ASP   A HB2  1 
ATOM   3432 H  HB2  B ASP   A 1 157 ? 8.079  1.232   1.705   0.30 25.71 ?  157 ASP   A HB2  1 
ATOM   3433 H  HB2  T ASP   A 1 157 ? 8.716  0.791   1.176   0.30 19.21 ?  157 ASP   A HB2  1 
ATOM   3434 H  HB3  A ASP   A 1 157 ? 7.869  -0.627  1.353   0.40 22.17 ?  157 ASP   A HB3  1 
ATOM   3435 H  HB3  B ASP   A 1 157 ? 7.557  -0.265  1.602   0.30 25.71 ?  157 ASP   A HB3  1 
ATOM   3436 H  HB3  T ASP   A 1 157 ? 7.987  -0.616  1.212   0.30 19.21 ?  157 ASP   A HB3  1 
ATOM   3437 N  N    A LYS   A 1 158 ? 5.721  -0.153  4.453   0.40 19.32 ?  158 LYS   A N    1 
ATOM   3438 N  N    B LYS   A 1 158 ? 5.304  -0.335  4.145   0.30 20.28 ?  158 LYS   A N    1 
ATOM   3439 N  N    T LYS   A 1 158 ? 5.811  -0.045  4.278   0.30 18.69 ?  158 LYS   A N    1 
ATOM   3440 C  CA   A LYS   A 1 158 ? 4.730  -1.065  5.024   0.40 20.27 ?  158 LYS   A CA   1 
ATOM   3441 C  CA   B LYS   A 1 158 ? 4.297  -1.243  4.690   0.30 20.26 ?  158 LYS   A CA   1 
ATOM   3442 C  CA   T LYS   A 1 158 ? 4.815  -0.913  4.904   0.30 20.17 ?  158 LYS   A CA   1 
ATOM   3443 C  C    A LYS   A 1 158 ? 3.972  -1.805  3.932   0.40 20.06 ?  158 LYS   A C    1 
ATOM   3444 C  C    B LYS   A 1 158 ? 3.676  -2.138  3.615   0.30 18.98 ?  158 LYS   A C    1 
ATOM   3445 C  C    T LYS   A 1 158 ? 4.034  -1.698  3.859   0.30 20.25 ?  158 LYS   A C    1 
ATOM   3446 O  O    A LYS   A 1 158 ? 3.732  -3.013  4.040   0.40 20.35 ?  158 LYS   A O    1 
ATOM   3447 O  O    B LYS   A 1 158 ? 3.674  -3.365  3.757   0.30 18.76 ?  158 LYS   A O    1 
ATOM   3448 O  O    T LYS   A 1 158 ? 3.783  -2.896  4.033   0.30 20.39 ?  158 LYS   A O    1 
ATOM   3449 C  CB   A LYS   A 1 158 ? 3.760  -0.309  5.938   0.40 21.74 ?  158 LYS   A CB   1 
ATOM   3450 C  CB   B LYS   A 1 158 ? 3.223  -0.435  5.435   0.30 21.55 ?  158 LYS   A CB   1 
ATOM   3451 C  CB   T LYS   A 1 158 ? 3.867  -0.097  5.787   0.30 21.94 ?  158 LYS   A CB   1 
ATOM   3452 C  CG   A LYS   A 1 158 ? 2.517  -1.108  6.364   0.40 23.31 ?  158 LYS   A CG   1 
ATOM   3453 C  CG   B LYS   A 1 158 ? 2.094  -1.263  6.052   0.30 22.89 ?  158 LYS   A CG   1 
ATOM   3454 C  CG   T LYS   A 1 158 ? 2.631  -0.866  6.264   0.30 23.53 ?  158 LYS   A CG   1 
ATOM   3455 C  CD   A LYS   A 1 158 ? 2.856  -2.394  7.127   0.40 24.55 ?  158 LYS   A CD   1 
ATOM   3456 C  CD   B LYS   A 1 158 ? 2.600  -2.251  7.098   0.30 24.01 ?  158 LYS   A CD   1 
ATOM   3457 C  CD   T LYS   A 1 158 ? 2.999  -2.086  7.104   0.30 24.98 ?  158 LYS   A CD   1 
ATOM   3458 C  CE   A LYS   A 1 158 ? 1.590  -3.061  7.666   0.40 25.16 ?  158 LYS   A CE   1 
ATOM   3459 C  CE   B LYS   A 1 158 ? 1.440  -2.954  7.797   0.30 24.55 ?  158 LYS   A CE   1 
ATOM   3460 C  CE   T LYS   A 1 158 ? 1.756  -2.878  7.501   0.30 25.93 ?  158 LYS   A CE   1 
ATOM   3461 N  NZ   A LYS   A 1 158 ? 1.836  -4.409  8.260   0.40 25.45 ?  158 LYS   A NZ   1 
ATOM   3462 N  NZ   B LYS   A 1 158 ? 1.864  -4.179  8.537   0.30 24.92 ?  158 LYS   A NZ   1 
ATOM   3463 N  NZ   T LYS   A 1 158 ? 2.079  -4.099  8.295   0.30 26.47 ?  158 LYS   A NZ   1 
ATOM   3464 H  H    A LYS   A 1 158 ? 5.612  0.673   4.655   0.40 23.16 ?  158 LYS   A H    1 
ATOM   3465 H  H    B LYS   A 1 158 ? 4.987  0.427   3.920   0.30 24.32 ?  158 LYS   A H    1 
ATOM   3466 H  H    T LYS   A 1 158 ? 5.704  0.793   4.436   0.30 22.41 ?  158 LYS   A H    1 
ATOM   3467 H  HA   A LYS   A 1 158 ? 5.189  -1.727  5.564   0.40 24.31 ?  158 LYS   A HA   1 
ATOM   3468 H  HA   B LYS   A 1 158 ? 4.721  -1.823  5.342   0.30 24.30 ?  158 LYS   A HA   1 
ATOM   3469 H  HA   T LYS   A 1 158 ? 5.269  -1.551  5.477   0.30 24.19 ?  158 LYS   A HA   1 
ATOM   3470 H  HB2  A LYS   A 1 158 ? 4.232  -0.045  6.745   0.40 26.07 ?  158 LYS   A HB2  1 
ATOM   3471 H  HB2  B LYS   A 1 158 ? 3.650  0.055   6.159   0.30 25.85 ?  158 LYS   A HB2  1 
ATOM   3472 H  HB2  T LYS   A 1 158 ? 4.349  0.198   6.579   0.30 26.31 ?  158 LYS   A HB2  1 
ATOM   3473 H  HB3  A LYS   A 1 158 ? 3.453  0.483   5.472   0.40 26.07 ?  158 LYS   A HB3  1 
ATOM   3474 H  HB3  B LYS   A 1 158 ? 2.820  0.193   4.816   0.30 25.85 ?  158 LYS   A HB3  1 
ATOM   3475 H  HB3  T LYS   A 1 158 ? 3.558  0.675   5.289   0.30 26.31 ?  158 LYS   A HB3  1 
ATOM   3476 H  HG2  A LYS   A 1 158 ? 1.978  -0.554  6.948   0.40 27.95 ?  158 LYS   A HG2  1 
ATOM   3477 H  HG2  B LYS   A 1 158 ? 1.464  -0.665  6.486   0.30 27.45 ?  158 LYS   A HG2  1 
ATOM   3478 H  HG2  T LYS   A 1 158 ? 2.091  -0.280  6.815   0.30 28.22 ?  158 LYS   A HG2  1 
ATOM   3479 H  HG3  A LYS   A 1 158 ? 2.001  -1.350  5.578   0.40 27.95 ?  158 LYS   A HG3  1 
ATOM   3480 H  HG3  B LYS   A 1 158 ? 1.645  -1.764  5.354   0.30 27.45 ?  158 LYS   A HG3  1 
ATOM   3481 H  HG3  T LYS   A 1 158 ? 2.112  -1.165  5.500   0.30 28.22 ?  158 LYS   A HG3  1 
ATOM   3482 H  HD2  A LYS   A 1 158 ? 3.300  -3.017  6.531   0.40 29.45 ?  158 LYS   A HD2  1 
ATOM   3483 H  HD2  B LYS   A 1 158 ? 3.150  -2.923  6.666   0.30 28.79 ?  158 LYS   A HD2  1 
ATOM   3484 H  HD2  T LYS   A 1 158 ? 3.578  -2.671  6.592   0.30 29.97 ?  158 LYS   A HD2  1 
ATOM   3485 H  HD3  A LYS   A 1 158 ? 3.428  -2.180  7.879   0.40 29.45 ?  158 LYS   A HD3  1 
ATOM   3486 H  HD3  B LYS   A 1 158 ? 3.117  -1.773  7.767   0.30 28.79 ?  158 LYS   A HD3  1 
ATOM   3487 H  HD3  T LYS   A 1 158 ? 3.445  -1.795  7.915   0.30 29.97 ?  158 LYS   A HD3  1 
ATOM   3488 H  HE2  A LYS   A 1 158 ? 1.205  -2.496  8.355   0.40 30.18 ?  158 LYS   A HE2  1 
ATOM   3489 H  HE2  B LYS   A 1 158 ? 1.043  -2.343  8.437   0.30 29.44 ?  158 LYS   A HE2  1 
ATOM   3490 H  HE2  T LYS   A 1 158 ? 1.177  -2.315  8.038   0.30 31.10 ?  158 LYS   A HE2  1 
ATOM   3491 H  HE3  A LYS   A 1 158 ? 0.959  -3.167  6.938   0.40 30.18 ?  158 LYS   A HE3  1 
ATOM   3492 H  HE3  B LYS   A 1 158 ? 0.780  -3.212  7.136   0.30 29.44 ?  158 LYS   A HE3  1 
ATOM   3493 H  HE3  T LYS   A 1 158 ? 1.291  -3.159  6.697   0.30 31.10 ?  158 LYS   A HE3  1 
ATOM   3494 H  HZ1  A LYS   A 1 158 ? 1.072  -4.754  8.559   0.40 30.52 ?  158 LYS   A HZ1  1 
ATOM   3495 H  HZ1  B LYS   A 1 158 ? 1.159  -4.558  8.928   0.30 29.89 ?  158 LYS   A HZ1  1 
ATOM   3496 H  HZ1  T LYS   A 1 158 ? 1.331  -4.533  8.506   0.30 31.75 ?  158 LYS   A HZ1  1 
ATOM   3497 H  HZ2  A LYS   A 1 158 ? 2.178  -4.954  7.645   0.40 30.52 ?  158 LYS   A HZ2  1 
ATOM   3498 H  HZ2  B LYS   A 1 158 ? 2.230  -4.764  7.974   0.30 29.89 ?  158 LYS   A HZ2  1 
ATOM   3499 H  HZ2  T LYS   A 1 158 ? 2.602  -4.641  7.820   0.30 31.75 ?  158 LYS   A HZ2  1 
ATOM   3500 H  HZ3  A LYS   A 1 158 ? 2.408  -4.343  8.938   0.40 30.52 ?  158 LYS   A HZ3  1 
ATOM   3501 H  HZ3  B LYS   A 1 158 ? 2.462  -3.967  9.161   0.30 29.89 ?  158 LYS   A HZ3  1 
ATOM   3502 H  HZ3  T LYS   A 1 158 ? 2.502  -3.872  9.044   0.30 31.75 ?  158 LYS   A HZ3  1 
ATOM   3503 N  N    A ASN   A 1 159 ? 3.581  -1.099  2.871   0.40 20.04 ?  159 ASN   A N    1 
ATOM   3504 N  N    B ASN   A 1 159 ? 3.139  -1.547  2.542   0.30 18.56 ?  159 ASN   A N    1 
ATOM   3505 N  N    T ASN   A 1 159 ? 3.631  -1.045  2.776   0.30 20.51 ?  159 ASN   A N    1 
ATOM   3506 C  CA   A ASN   A 1 159 ? 2.874  -1.764  1.783   0.40 20.03 ?  159 ASN   A CA   1 
ATOM   3507 C  CA   B ASN   A 1 159 ? 2.625  -2.352  1.435   0.30 18.21 ?  159 ASN   A CA   1 
ATOM   3508 C  CA   T ASN   A 1 159 ? 2.887  -1.726  1.725   0.30 20.78 ?  159 ASN   A CA   1 
ATOM   3509 C  C    A ASN   A 1 159 ? 3.738  -2.842  1.138   0.40 19.34 ?  159 ASN   A C    1 
ATOM   3510 C  C    B ASN   A 1 159 ? 3.653  -3.387  1.007   0.30 17.47 ?  159 ASN   A C    1 
ATOM   3511 C  C    T ASN   A 1 159 ? 3.714  -2.828  1.072   0.30 20.85 ?  159 ASN   A C    1 
ATOM   3512 O  O    A ASN   A 1 159 ? 3.252  -3.939  0.843   0.40 19.20 ?  159 ASN   A O    1 
ATOM   3513 O  O    B ASN   A 1 159 ? 3.321  -4.555  0.769   0.30 17.31 ?  159 ASN   A O    1 
ATOM   3514 O  O    T ASN   A 1 159 ? 3.176  -3.864  0.690   0.30 20.73 ?  159 ASN   A O    1 
ATOM   3515 C  CB   A ASN   A 1 159 ? 2.389  -0.737  0.760   0.40 20.87 ?  159 ASN   A CB   1 
ATOM   3516 C  CB   B ASN   A 1 159 ? 2.277  -1.448  0.249   0.30 18.79 ?  159 ASN   A CB   1 
ATOM   3517 C  CB   T ASN   A 1 159 ? 2.389  -0.732  0.675   0.30 21.23 ?  159 ASN   A CB   1 
ATOM   3518 C  CG   A ASN   A 1 159 ? 1.186  0.050   1.252   0.40 22.00 ?  159 ASN   A CG   1 
ATOM   3519 C  CG   B ASN   A 1 159 ? 0.833  -0.996  0.259   0.30 19.43 ?  159 ASN   A CG   1 
ATOM   3520 C  CG   T ASN   A 1 159 ? 1.198  0.077   1.159   0.30 21.84 ?  159 ASN   A CG   1 
ATOM   3521 O  OD1  A ASN   A 1 159 ? 0.367  -0.465  2.011   0.40 22.88 ?  159 ASN   A OD1  1 
ATOM   3522 O  OD1  B ASN   A 1 159 ? 0.188  -0.957  1.305   0.30 20.20 ?  159 ASN   A OD1  1 
ATOM   3523 O  OD1  T ASN   A 1 159 ? 0.401  -0.397  1.968   0.30 22.44 ?  159 ASN   A OD1  1 
ATOM   3524 N  ND2  A ASN   A 1 159 ? 1.074  1.300   0.823   0.40 22.42 ?  159 ASN   A ND2  1 
ATOM   3525 N  ND2  B ASN   A 1 159 ? 0.315  -0.652  -0.917  0.30 19.45 ?  159 ASN   A ND2  1 
ATOM   3526 N  ND2  T ASN   A 1 159 ? 1.070  1.300   0.666   0.30 22.07 ?  159 ASN   A ND2  1 
ATOM   3527 H  H    A ASN   A 1 159 ? 3.707  -0.257  2.765   0.40 24.03 ?  159 ASN   A H    1 
ATOM   3528 H  H    B ASN   A 1 159 ? 3.074  -0.698  2.430   0.30 22.26 ?  159 ASN   A H    1 
ATOM   3529 H  H    T ASN   A 1 159 ? 3.768  -0.210  2.632   0.30 24.59 ?  159 ASN   A H    1 
ATOM   3530 H  HA   A ASN   A 1 159 ? 2.091  -2.203  2.150   0.40 24.01 ?  159 ASN   A HA   1 
ATOM   3531 H  HA   B ASN   A 1 159 ? 1.819  -2.813  1.713   0.30 21.83 ?  159 ASN   A HA   1 
ATOM   3532 H  HA   T ASN   A 1 159 ? 2.112  -2.150  2.122   0.30 24.92 ?  159 ASN   A HA   1 
ATOM   3533 H  HB2  A ASN   A 1 159 ? 3.100  -0.108  0.577   0.40 25.02 ?  159 ASN   A HB2  1 
ATOM   3534 H  HB2  B ASN   A 1 159 ? 2.839  -0.655  0.278   0.30 22.53 ?  159 ASN   A HB2  1 
ATOM   3535 H  HB2  T ASN   A 1 159 ? 3.102  -0.115  0.459   0.30 25.47 ?  159 ASN   A HB2  1 
ATOM   3536 H  HB3  A ASN   A 1 159 ? 2.135  -1.201  -0.056  0.40 25.02 ?  159 ASN   A HB3  1 
ATOM   3537 H  HB3  B ASN   A 1 159 ? 2.432  -1.931  -0.576  0.30 22.53 ?  159 ASN   A HB3  1 
ATOM   3538 H  HB3  T ASN   A 1 159 ? 2.122  -1.224  -0.120  0.30 25.47 ?  159 ASN   A HB3  1 
ATOM   3539 H  HD21 A ASN   A 1 159 ? 0.406  1.780   1.072   0.40 26.89 ?  159 ASN   A HD21 1 
ATOM   3540 H  HD21 B ASN   A 1 159 ? -0.500 -0.384  -0.969  0.30 23.32 ?  159 ASN   A HD21 1 
ATOM   3541 H  HD21 T ASN   A 1 159 ? 0.409  1.791   0.909   0.30 26.46 ?  159 ASN   A HD21 1 
ATOM   3542 H  HD22 A ASN   A 1 159 ? 1.669  1.627   0.299   0.40 26.89 ?  159 ASN   A HD22 1 
ATOM   3543 H  HD22 B ASN   A 1 159 ? 0.797  -0.697  -1.630  0.30 23.32 ?  159 ASN   A HD22 1 
ATOM   3544 H  HD22 T ASN   A 1 159 ? 1.649  1.597   0.107   0.30 26.46 ?  159 ASN   A HD22 1 
ATOM   3545 N  N    A LEU   A 1 160 ? 5.026  -2.563  0.930   0.40 18.24 ?  160 LEU   A N    1 
ATOM   3546 N  N    B LEU   A 1 160 ? 4.914  -2.966  0.912   0.30 17.24 ?  160 LEU   A N    1 
ATOM   3547 N  N    T LEU   A 1 160 ? 5.019  -2.614  0.948   0.30 20.77 ?  160 LEU   A N    1 
ATOM   3548 C  CA   A LEU   A 1 160 ? 5.898  -3.586  0.360   0.40 16.90 ?  160 LEU   A CA   1 
ATOM   3549 C  CA   B LEU   A 1 160 ? 5.990  -3.884  0.568   0.30 16.72 ?  160 LEU   A CA   1 
ATOM   3550 C  CA   T LEU   A 1 160 ? 5.889  -3.642  0.391   0.30 20.40 ?  160 LEU   A CA   1 
ATOM   3551 C  C    A LEU   A 1 160 ? 6.079  -4.758  1.316   0.40 15.37 ?  160 LEU   A C    1 
ATOM   3552 C  C    B LEU   A 1 160 ? 6.142  -4.969  1.626   0.30 15.58 ?  160 LEU   A C    1 
ATOM   3553 O  O    A LEU   A 1 160 ? 6.100  -5.917  0.888   0.40 14.78 ?  160 LEU   A O    1 
ATOM   3554 O  O    B LEU   A 1 160 ? 6.149  -6.164  1.310   0.30 15.27 ?  160 LEU   A O    1 
ATOM   3555 C  CB   A LEU   A 1 160 ? 7.254  -2.988  -0.004  0.40 16.75 ?  160 LEU   A CB   1 
ATOM   3556 C  CB   B LEU   A 1 160 ? 7.292  -3.098  0.419   0.30 17.31 ?  160 LEU   A CB   1 
ATOM   3557 C  CB   T LEU   A 1 160 ? 7.261  -3.069  0.044   0.30 19.92 ?  160 LEU   A CB   1 
ATOM   3558 C  CG   A LEU   A 1 160 ? 8.296  -4.024  -0.423  0.40 17.64 ?  160 LEU   A CG   1 
ATOM   3559 C  CG   B LEU   A 1 160 ? 8.485  -3.963  0.036   0.30 17.94 ?  160 LEU   A CG   1 
ATOM   3560 C  CG   T LEU   A 1 160 ? 8.296  -4.105  -0.392  0.30 19.88 ?  160 LEU   A CG   1 
ATOM   3561 C  CD1  A LEU   A 1 160 ? 7.817  -4.802  -1.635  0.40 18.30 ?  160 LEU   A CD1  1 
ATOM   3562 C  CD1  B LEU   A 1 160 ? 8.125  -4.757  -1.197  0.30 18.33 ?  160 LEU   A CD1  1 
ATOM   3563 C  CD1  T LEU   A 1 160 ? 7.824  -4.853  -1.625  0.30 20.08 ?  160 LEU   A CD1  1 
ATOM   3564 C  CD2  A LEU   A 1 160 ? 9.626  -3.356  -0.698  0.40 17.74 ?  160 LEU   A CD2  1 
ATOM   3565 C  CD2  B LEU   A 1 160 ? 9.721  -3.114  -0.205  0.30 17.93 ?  160 LEU   A CD2  1 
ATOM   3566 C  CD2  T LEU   A 1 160 ? 9.636  -3.438  -0.649  0.30 19.68 ?  160 LEU   A CD2  1 
ATOM   3567 H  H    A LEU   A 1 160 ? 5.407  -1.811  1.110   0.40 21.88 ?  160 LEU   A H    1 
ATOM   3568 H  H    B LEU   A 1 160 ? 5.169  -2.156  1.039   0.30 20.67 ?  160 LEU   A H    1 
ATOM   3569 H  H    T LEU   A 1 160 ? 5.425  -1.888  1.177   0.30 24.90 ?  160 LEU   A H    1 
ATOM   3570 H  HA   A LEU   A 1 160 ? 5.493  -3.921  -0.450  0.40 20.26 ?  160 LEU   A HA   1 
ATOM   3571 H  HA   B LEU   A 1 160 ? 5.776  -4.304  -0.281  0.30 20.05 ?  160 LEU   A HA   1 
ATOM   3572 H  HB2  A LEU   A 1 160 ? 7.141  -2.352  -0.733  0.40 20.09 ?  160 LEU   A HB2  1 
ATOM   3573 H  HB2  B LEU   A 1 160 ? 7.181  -2.425  -0.273  0.30 20.76 ?  160 LEU   A HB2  1 
ATOM   3574 H  HB2  T LEU   A 1 160 ? 7.158  -2.425  -0.677  0.30 23.89 ?  160 LEU   A HB2  1 
ATOM   3575 H  HB3  A LEU   A 1 160 ? 7.605  -2.537  0.776   0.40 20.09 ?  160 LEU   A HB3  1 
ATOM   3576 H  HB3  B LEU   A 1 160 ? 7.498  -2.665  1.265   0.30 20.76 ?  160 LEU   A HB3  1 
ATOM   3577 H  HB3  T LEU   A 1 160 ? 7.617  -2.627  0.830   0.30 23.89 ?  160 LEU   A HB3  1 
ATOM   3578 H  HG   A LEU   A 1 160 ? 8.436  -4.650  0.304   0.40 21.15 ?  160 LEU   A HG   1 
ATOM   3579 H  HG   B LEU   A 1 160 ? 8.681  -4.584  0.756   0.30 21.52 ?  160 LEU   A HG   1 
ATOM   3580 H  HG   T LEU   A 1 160 ? 8.418  -4.748  0.325   0.30 23.84 ?  160 LEU   A HG   1 
ATOM   3581 H  HD11 A LEU   A 1 160 ? 8.538  -5.373  -1.942  0.40 21.94 ?  160 LEU   A HD11 1 
ATOM   3582 H  HD11 B LEU   A 1 160 ? 8.928  -5.146  -1.556  0.30 21.98 ?  160 LEU   A HD11 1 
ATOM   3583 H  HD11 T LEU   A 1 160 ? 8.538  -5.434  -1.931  0.30 24.09 ?  160 LEU   A HD11 1 
ATOM   3584 H  HD12 A LEU   A 1 160 ? 7.052  -5.341  -1.383  0.40 21.94 ?  160 LEU   A HD12 1 
ATOM   3585 H  HD12 B LEU   A 1 160 ? 7.500  -5.458  -0.954  0.30 21.98 ?  160 LEU   A HD12 1 
ATOM   3586 H  HD12 T LEU   A 1 160 ? 7.044  -5.380  -1.393  0.30 24.09 ?  160 LEU   A HD12 1 
ATOM   3587 H  HD13 A LEU   A 1 160 ? 7.569  -4.176  -2.332  0.40 21.94 ?  160 LEU   A HD13 1 
ATOM   3588 H  HD13 B LEU   A 1 160 ? 7.719  -4.159  -1.848  0.30 21.98 ?  160 LEU   A HD13 1 
ATOM   3589 H  HD13 T LEU   A 1 160 ? 7.600  -4.210  -2.315  0.30 24.09 ?  160 LEU   A HD13 1 
ATOM   3590 H  HD21 A LEU   A 1 160 ? 10.270 -4.034  -0.957  0.40 21.28 ?  160 LEU   A HD21 1 
ATOM   3591 H  HD21 B LEU   A 1 160 ? 10.462 -3.695  -0.442  0.30 21.50 ?  160 LEU   A HD21 1 
ATOM   3592 H  HD21 T LEU   A 1 160 ? 10.277 -4.113  -0.921  0.30 23.61 ?  160 LEU   A HD21 1 
ATOM   3593 H  HD22 A LEU   A 1 160 ? 9.515  -2.713  -1.415  0.40 21.28 ?  160 LEU   A HD22 1 
ATOM   3594 H  HD22 B LEU   A 1 160 ? 9.543  -2.494  -0.929  0.30 21.50 ?  160 LEU   A HD22 1 
ATOM   3595 H  HD22 T LEU   A 1 160 ? 9.530  -2.779  -1.352  0.30 23.61 ?  160 LEU   A HD22 1 
ATOM   3596 H  HD23 A LEU   A 1 160 ? 9.928  -2.905  0.108   0.40 21.28 ?  160 LEU   A HD23 1 
ATOM   3597 H  HD23 B LEU   A 1 160 ? 9.934  -2.624  0.605   0.30 21.50 ?  160 LEU   A HD23 1 
ATOM   3598 H  HD23 T LEU   A 1 160 ? 9.936  -3.007  0.167   0.30 23.61 ?  160 LEU   A HD23 1 
ATOM   3599 N  N    A TYR   A 1 161 ? 6.229  -4.472  2.610   0.70 16.41 ?  161 TYR   A N    1 
ATOM   3600 N  N    B TYR   A 1 161 ? 6.275  -4.567  2.894   0.30 16.00 ?  161 TYR   A N    1 
ATOM   3601 C  CA   A TYR   A 1 161 ? 6.364  -5.534  3.602   0.70 16.05 ?  161 TYR   A CA   1 
ATOM   3602 C  CA   B TYR   A 1 161 ? 6.406  -5.541  3.974   0.30 15.59 ?  161 TYR   A CA   1 
ATOM   3603 C  C    A TYR   A 1 161 ? 5.210  -6.526  3.522   0.70 16.57 ?  161 TYR   A C    1 
ATOM   3604 C  C    B TYR   A 1 161 ? 5.246  -6.530  3.967   0.30 15.92 ?  161 TYR   A C    1 
ATOM   3605 O  O    A TYR   A 1 161 ? 5.418  -7.744  3.523   0.70 15.81 ?  161 TYR   A O    1 
ATOM   3606 O  O    B TYR   A 1 161 ? 5.449  -7.746  4.045   0.30 15.42 ?  161 TYR   A O    1 
ATOM   3607 C  CB   A TYR   A 1 161 ? 6.440  -4.928  5.001   0.70 15.77 ?  161 TYR   A CB   1 
ATOM   3608 C  CB   B TYR   A 1 161 ? 6.501  -4.828  5.326   0.30 15.65 ?  161 TYR   A CB   1 
ATOM   3609 C  CG   A TYR   A 1 161 ? 6.337  -5.956  6.098   0.70 14.73 ?  161 TYR   A CG   1 
ATOM   3610 C  CG   B TYR   A 1 161 ? 6.381  -5.764  6.510   0.30 15.22 ?  161 TYR   A CG   1 
ATOM   3611 C  CD1  A TYR   A 1 161 ? 7.453  -6.669  6.506   0.70 14.49 ?  161 TYR   A CD1  1 
ATOM   3612 C  CD1  B TYR   A 1 161 ? 7.485  -6.456  6.995   0.30 15.05 ?  161 TYR   A CD1  1 
ATOM   3613 C  CD2  A TYR   A 1 161 ? 5.125  -6.215  6.731   0.70 14.78 ?  161 TYR   A CD2  1 
ATOM   3614 C  CD2  B TYR   A 1 161 ? 5.160  -5.957  7.143   0.30 14.97 ?  161 TYR   A CD2  1 
ATOM   3615 C  CE1  A TYR   A 1 161 ? 7.368  -7.617  7.504   0.70 13.92 ?  161 TYR   A CE1  1 
ATOM   3616 C  CE1  B TYR   A 1 161 ? 7.373  -7.316  8.074   0.30 15.24 ?  161 TYR   A CE1  1 
ATOM   3617 C  CE2  A TYR   A 1 161 ? 5.031  -7.166  7.734   0.70 14.11 ?  161 TYR   A CE2  1 
ATOM   3618 C  CE2  B TYR   A 1 161 ? 5.039  -6.814  8.221   0.30 15.19 ?  161 TYR   A CE2  1 
ATOM   3619 C  CZ   A TYR   A 1 161 ? 6.159  -7.863  8.115   0.70 14.22 ?  161 TYR   A CZ   1 
ATOM   3620 C  CZ   B TYR   A 1 161 ? 6.147  -7.489  8.683   0.30 15.75 ?  161 TYR   A CZ   1 
ATOM   3621 O  OH   A TYR   A 1 161 ? 6.094  -8.809  9.111   0.70 14.42 ?  161 TYR   A OH   1 
ATOM   3622 O  OH   B TYR   A 1 161 ? 6.021  -8.341  9.758   0.30 16.72 ?  161 TYR   A OH   1 
ATOM   3623 H  H    A TYR   A 1 161 ? 6.247  -3.681  2.940   0.70 19.68 ?  161 TYR   A H    1 
ATOM   3624 H  H    B TYR   A 1 161 ? 6.293  -3.745  3.145   0.30 19.19 ?  161 TYR   A H    1 
ATOM   3625 H  HA   A TYR   A 1 161 ? 7.180  -6.023  3.440   0.70 19.25 ?  161 TYR   A HA   1 
ATOM   3626 H  HA   B TYR   A 1 161 ? 7.224  -6.041  3.844   0.30 18.69 ?  161 TYR   A HA   1 
ATOM   3627 H  HB2  A TYR   A 1 161 ? 7.292  -4.477  5.101   0.70 18.91 ?  161 TYR   A HB2  1 
ATOM   3628 H  HB2  B TYR   A 1 161 ? 7.360  -4.382  5.385   0.30 18.77 ?  161 TYR   A HB2  1 
ATOM   3629 H  HB3  A TYR   A 1 161 ? 5.713  -4.298  5.117   0.70 18.91 ?  161 TYR   A HB3  1 
ATOM   3630 H  HB3  B TYR   A 1 161 ? 5.786  -4.175  5.388   0.30 18.77 ?  161 TYR   A HB3  1 
ATOM   3631 H  HD1  A TYR   A 1 161 ? 8.270  -6.514  6.097   0.70 17.37 ?  161 TYR   A HD1  1 
ATOM   3632 H  HD1  B TYR   A 1 161 ? 8.312  -6.341  6.587   0.30 18.05 ?  161 TYR   A HD1  1 
ATOM   3633 H  HD2  A TYR   A 1 161 ? 4.360  -5.754  6.476   0.70 17.72 ?  161 TYR   A HD2  1 
ATOM   3634 H  HD2  B TYR   A 1 161 ? 4.407  -5.506  6.836   0.30 17.95 ?  161 TYR   A HD2  1 
ATOM   3635 H  HE1  A TYR   A 1 161 ? 8.124  -8.093  7.766   0.70 16.69 ?  161 TYR   A HE1  1 
ATOM   3636 H  HE1  B TYR   A 1 161 ? 8.120  -7.773  8.392   0.30 18.28 ?  161 TYR   A HE1  1 
ATOM   3637 H  HE2  A TYR   A 1 161 ? 4.208  -7.335  8.148   0.70 16.92 ?  161 TYR   A HE2  1 
ATOM   3638 H  HE2  B TYR   A 1 161 ? 4.211  -6.932  8.635   0.30 18.21 ?  161 TYR   A HE2  1 
ATOM   3639 H  HH   A TYR   A 1 161 ? 6.844  -9.159  9.235   0.70 17.29 ?  161 TYR   A HH   1 
ATOM   3640 H  HH   B TYR   A 1 161 ? 6.759  -8.688  9.943   0.30 20.04 ?  161 TYR   A HH   1 
ATOM   3641 N  N    A ASP   A 1 162 ? 3.976  -6.021  3.480   0.70 17.55 ?  162 ASP   A N    1 
ATOM   3642 N  N    B ASP   A 1 162 ? 4.015  -6.023  3.880   0.30 16.96 ?  162 ASP   A N    1 
ATOM   3643 C  CA   A ASP   A 1 162 ? 2.820  -6.912  3.416   0.70 18.55 ?  162 ASP   A CA   1 
ATOM   3644 C  CA   B ASP   A 1 162 ? 2.857  -6.913  3.870   0.30 17.89 ?  162 ASP   A CA   1 
ATOM   3645 C  C    A ASP   A 1 162 ? 2.865  -7.767  2.158   0.70 18.38 ?  162 ASP   A C    1 
ATOM   3646 C  C    B ASP   A 1 162 ? 2.870  -7.820  2.646   0.30 18.04 ?  162 ASP   A C    1 
ATOM   3647 O  O    A ASP   A 1 162 ? 2.537  -8.959  2.193   0.70 18.67 ?  162 ASP   A O    1 
ATOM   3648 O  O    B ASP   A 1 162 ? 2.469  -8.987  2.723   0.30 17.75 ?  162 ASP   A O    1 
ATOM   3649 C  CB   A ASP   A 1 162 ? 1.518  -6.106  3.460   0.70 20.29 ?  162 ASP   A CB   1 
ATOM   3650 C  CB   B ASP   A 1 162 ? 1.564  -6.099  3.927   0.30 18.74 ?  162 ASP   A CB   1 
ATOM   3651 C  CG   A ASP   A 1 162 ? 1.207  -5.547  4.836   0.70 22.18 ?  162 ASP   A CG   1 
ATOM   3652 C  CG   B ASP   A 1 162 ? 1.347  -5.441  5.276   0.30 19.77 ?  162 ASP   A CG   1 
ATOM   3653 O  OD1  A ASP   A 1 162 ? 1.798  -6.003  5.834   0.70 22.89 ?  162 ASP   A OD1  1 
ATOM   3654 O  OD1  B ASP   A 1 162 ? 2.119  -5.726  6.215   0.30 20.32 ?  162 ASP   A OD1  1 
ATOM   3655 O  OD2  A ASP   A 1 162 ? 0.330  -4.657  4.914   0.70 23.41 -1 162 ASP   A OD2  1 
ATOM   3656 O  OD2  B ASP   A 1 162 ? 0.396  -4.640  5.397   0.30 20.50 -1 162 ASP   A OD2  1 
ATOM   3657 H  H    A ASP   A 1 162 ? 3.777  -5.186  3.489   0.70 21.04 ?  162 ASP   A H    1 
ATOM   3658 H  H    B ASP   A 1 162 ? 3.828  -5.185  3.827   0.30 20.33 ?  162 ASP   A H    1 
ATOM   3659 H  HA   A ASP   A 1 162 ? 2.825  -7.510  4.179   0.70 22.25 ?  162 ASP   A HA   1 
ATOM   3660 H  HA   B ASP   A 1 162 ? 2.887  -7.476  4.655   0.30 21.45 ?  162 ASP   A HA   1 
ATOM   3661 H  HB2  A ASP   A 1 162 ? 1.588  -5.352  2.860   0.70 24.34 ?  162 ASP   A HB2  1 
ATOM   3662 H  HB2  B ASP   A 1 162 ? 1.594  -5.399  3.256   0.30 22.47 ?  162 ASP   A HB2  1 
ATOM   3663 H  HB3  A ASP   A 1 162 ? 0.776  -6.675  3.202   0.70 24.34 ?  162 ASP   A HB3  1 
ATOM   3664 H  HB3  B ASP   A 1 162 ? 0.810  -6.687  3.758   0.30 22.47 ?  162 ASP   A HB3  1 
ATOM   3665 N  N    A LYS   A 1 163 ? 3.277  -7.175  1.037   0.70 19.04 ?  163 LYS   A N    1 
ATOM   3666 N  N    B LYS   A 1 163 ? 3.333  -7.301  1.507   0.30 18.71 ?  163 LYS   A N    1 
ATOM   3667 C  CA   A LYS   A 1 163 ? 3.395  -7.938  -0.199  0.70 19.91 ?  163 LYS   A CA   1 
ATOM   3668 C  CA   B LYS   A 1 163 ? 3.373  -8.102  0.287   0.30 19.39 ?  163 LYS   A CA   1 
ATOM   3669 C  C    A LYS   A 1 163 ? 4.470  -9.012  -0.084  0.70 19.39 ?  163 LYS   A C    1 
ATOM   3670 C  C    B LYS   A 1 163 ? 4.500  -9.129  0.334   0.30 18.57 ?  163 LYS   A C    1 
ATOM   3671 O  O    A LYS   A 1 163 ? 4.311  -10.119 -0.608  0.70 19.90 ?  163 LYS   A O    1 
ATOM   3672 O  O    B LYS   A 1 163 ? 4.336  -10.258 -0.143  0.30 18.71 ?  163 LYS   A O    1 
ATOM   3673 C  CB   A LYS   A 1 163 ? 3.700  -6.994  -1.362  0.70 22.60 ?  163 LYS   A CB   1 
ATOM   3674 C  CB   B LYS   A 1 163 ? 3.509  -7.175  -0.920  0.30 21.38 ?  163 LYS   A CB   1 
ATOM   3675 C  CG   A LYS   A 1 163 ? 3.800  -7.694  -2.701  0.70 25.76 ?  163 LYS   A CG   1 
ATOM   3676 C  CG   B LYS   A 1 163 ? 3.487  -7.857  -2.270  0.30 23.16 ?  163 LYS   A CG   1 
ATOM   3677 C  CD   A LYS   A 1 163 ? 4.217  -6.739  -3.798  0.70 28.92 ?  163 LYS   A CD   1 
ATOM   3678 C  CD   B LYS   A 1 163 ? 3.406  -6.805  -3.364  0.30 24.65 ?  163 LYS   A CD   1 
ATOM   3679 C  CE   A LYS   A 1 163 ? 4.163  -7.417  -5.155  0.70 31.26 ?  163 LYS   A CE   1 
ATOM   3680 C  CE   B LYS   A 1 163 ? 3.875  -7.333  -4.705  0.30 25.92 ?  163 LYS   A CE   1 
ATOM   3681 N  NZ   A LYS   A 1 163 ? 4.832  -6.609  -6.207  0.70 32.60 ?  163 LYS   A NZ   1 
ATOM   3682 N  NZ   B LYS   A 1 163 ? 4.196  -6.216  -5.639  0.30 26.42 ?  163 LYS   A NZ   1 
ATOM   3683 H  H    A LYS   A 1 163 ? 3.483  -6.340  0.969   0.70 22.83 ?  163 LYS   A H    1 
ATOM   3684 H  H    B LYS   A 1 163 ? 3.622  -6.497  1.413   0.30 22.44 ?  163 LYS   A H    1 
ATOM   3685 H  HA   A LYS   A 1 163 ? 2.546  -8.371  -0.384  0.70 23.88 ?  163 LYS   A HA   1 
ATOM   3686 H  HA   B LYS   A 1 163 ? 2.539  -8.584  0.197   0.30 23.25 ?  163 LYS   A HA   1 
ATOM   3687 H  HB2  A LYS   A 1 163 ? 2.989  -6.332  -1.427  0.70 27.10 ?  163 LYS   A HB2  1 
ATOM   3688 H  HB2  B LYS   A 1 163 ? 2.772  -6.542  -0.907  0.30 25.64 ?  163 LYS   A HB2  1 
ATOM   3689 H  HB3  A LYS   A 1 163 ? 4.544  -6.551  -1.194  0.70 27.10 ?  163 LYS   A HB3  1 
ATOM   3690 H  HB3  B LYS   A 1 163 ? 4.348  -6.696  -0.852  0.30 25.64 ?  163 LYS   A HB3  1 
ATOM   3691 H  HG2  A LYS   A 1 163 ? 4.462  -8.400  -2.649  0.70 30.89 ?  163 LYS   A HG2  1 
ATOM   3692 H  HG2  B LYS   A 1 163 ? 4.303  -8.369  -2.389  0.30 27.77 ?  163 LYS   A HG2  1 
ATOM   3693 H  HG3  A LYS   A 1 163 ? 2.932  -8.065  -2.932  0.70 30.89 ?  163 LYS   A HG3  1 
ATOM   3694 H  HG3  B LYS   A 1 163 ? 2.709  -8.434  -2.334  0.30 27.77 ?  163 LYS   A HG3  1 
ATOM   3695 H  HD2  A LYS   A 1 163 ? 3.612  -5.980  -3.810  0.70 34.69 ?  163 LYS   A HD2  1 
ATOM   3696 H  HD2  B LYS   A 1 163 ? 2.484  -6.517  -3.459  0.30 29.57 ?  163 LYS   A HD2  1 
ATOM   3697 H  HD3  A LYS   A 1 163 ? 5.126  -6.443  -3.636  0.70 34.69 ?  163 LYS   A HD3  1 
ATOM   3698 H  HD3  B LYS   A 1 163 ? 3.966  -6.052  -3.121  0.30 29.57 ?  163 LYS   A HD3  1 
ATOM   3699 H  HE2  A LYS   A 1 163 ? 4.602  -8.279  -5.098  0.70 37.50 ?  163 LYS   A HE2  1 
ATOM   3700 H  HE2  B LYS   A 1 163 ? 4.675  -7.863  -4.575  0.30 31.09 ?  163 LYS   A HE2  1 
ATOM   3701 H  HE3  A LYS   A 1 163 ? 3.236  -7.535  -5.411  0.70 37.50 ?  163 LYS   A HE3  1 
ATOM   3702 H  HE3  B LYS   A 1 163 ? 3.175  -7.872  -5.103  0.30 31.09 ?  163 LYS   A HE3  1 
ATOM   3703 H  HZ1  A LYS   A 1 163 ? 4.786  -7.031  -6.988  0.70 39.11 ?  163 LYS   A HZ1  1 
ATOM   3704 H  HZ1  B LYS   A 1 163 ? 4.471  -6.541  -6.420  0.30 31.69 ?  163 LYS   A HZ1  1 
ATOM   3705 H  HZ2  A LYS   A 1 163 ? 4.432  -5.817  -6.280  0.70 39.11 ?  163 LYS   A HZ2  1 
ATOM   3706 H  HZ2  B LYS   A 1 163 ? 3.474  -5.713  -5.773  0.30 31.69 ?  163 LYS   A HZ2  1 
ATOM   3707 H  HZ3  A LYS   A 1 163 ? 5.687  -6.483  -5.995  0.70 39.11 ?  163 LYS   A HZ3  1 
ATOM   3708 H  HZ3  B LYS   A 1 163 ? 4.842  -5.707  -5.295  0.30 31.69 ?  163 LYS   A HZ3  1 
ATOM   3709 N  N    A LEU   A 1 164 ? 5.582  -8.697  0.583   0.70 17.81 ?  164 LEU   A N    1 
ATOM   3710 N  N    B LEU   A 1 164 ? 5.649  -8.760  0.908   0.30 17.44 ?  164 LEU   A N    1 
ATOM   3711 C  CA   A LEU   A 1 164 ? 6.661  -9.671  0.726   0.70 16.88 ?  164 LEU   A CA   1 
ATOM   3712 C  CA   B LEU   A 1 164 ? 6.740  -9.719  1.060   0.30 16.50 ?  164 LEU   A CA   1 
ATOM   3713 C  C    A LEU   A 1 164 ? 6.228  -10.849 1.589   0.70 16.98 ?  164 LEU   A C    1 
ATOM   3714 C  C    B LEU   A 1 164 ? 6.311  -10.891 1.931   0.30 16.49 ?  164 LEU   A C    1 
ATOM   3715 O  O    A LEU   A 1 164 ? 6.510  -12.007 1.259   0.70 17.44 ?  164 LEU   A O    1 
ATOM   3716 O  O    B LEU   A 1 164 ? 6.639  -12.048 1.641   0.30 16.77 ?  164 LEU   A O    1 
ATOM   3717 C  CB   A LEU   A 1 164 ? 7.887  -8.994  1.331   0.70 16.33 ?  164 LEU   A CB   1 
ATOM   3718 C  CB   B LEU   A 1 164 ? 7.956  -9.028  1.680   0.30 15.79 ?  164 LEU   A CB   1 
ATOM   3719 C  CG   A LEU   A 1 164 ? 8.646  -8.034  0.414   0.70 16.16 ?  164 LEU   A CG   1 
ATOM   3720 C  CG   B LEU   A 1 164 ? 8.724  -8.013  0.832   0.30 15.47 ?  164 LEU   A CG   1 
ATOM   3721 C  CD1  A LEU   A 1 164 ? 9.583  -7.160  1.231   0.70 15.77 ?  164 LEU   A CD1  1 
ATOM   3722 C  CD1  B LEU   A 1 164 ? 9.630  -7.174  1.722   0.30 15.28 ?  164 LEU   A CD1  1 
ATOM   3723 C  CD2  A LEU   A 1 164 ? 9.426  -8.795  -0.644  0.70 16.72 ?  164 LEU   A CD2  1 
ATOM   3724 C  CD2  B LEU   A 1 164 ? 9.539  -8.713  -0.243  0.30 15.35 ?  164 LEU   A CD2  1 
ATOM   3725 H  H    A LEU   A 1 164 ? 5.734  -7.933  0.956   0.70 21.35 ?  164 LEU   A H    1 
ATOM   3726 H  H    B LEU   A 1 164 ? 5.815  -7.978  1.222   0.30 20.91 ?  164 LEU   A H    1 
ATOM   3727 H  HA   A LEU   A 1 164 ? 6.899  -10.007 -0.150  0.70 20.24 ?  164 LEU   A HA   1 
ATOM   3728 H  HA   B LEU   A 1 164 ? 6.996  -10.062 0.189   0.30 19.78 ?  164 LEU   A HA   1 
ATOM   3729 H  HB2  A LEU   A 1 164 ? 7.606  -8.487  2.107   0.70 19.57 ?  164 LEU   A HB2  1 
ATOM   3730 H  HB2  B LEU   A 1 164 ? 7.661  -8.560  2.474   0.30 18.94 ?  164 LEU   A HB2  1 
ATOM   3731 H  HB3  A LEU   A 1 164 ? 8.511  -9.683  1.603   0.70 19.57 ?  164 LEU   A HB3  1 
ATOM   3732 H  HB3  B LEU   A 1 164 ? 8.593  -9.714  1.934   0.30 18.94 ?  164 LEU   A HB3  1 
ATOM   3733 H  HG   A LEU   A 1 164 ? 8.012  -7.453  -0.036  0.70 19.37 ?  164 LEU   A HG   1 
ATOM   3734 H  HG   B LEU   A 1 164 ? 8.097  -7.416  0.396   0.30 18.54 ?  164 LEU   A HG   1 
ATOM   3735 H  HD11 A LEU   A 1 164 ? 10.057 -6.560  0.636   0.70 18.90 ?  164 LEU   A HD11 1 
ATOM   3736 H  HD11 B LEU   A 1 164 ? 10.113 -6.538  1.173   0.30 18.32 ?  164 LEU   A HD11 1 
ATOM   3737 H  HD12 A LEU   A 1 164 ? 9.059  -6.648  1.870   0.70 18.90 ?  164 LEU   A HD12 1 
ATOM   3738 H  HD12 B LEU   A 1 164 ? 9.084  -6.703  2.372   0.30 18.32 ?  164 LEU   A HD12 1 
ATOM   3739 H  HD13 A LEU   A 1 164 ? 10.213 -7.728  1.702   0.70 18.90 ?  164 LEU   A HD13 1 
ATOM   3740 H  HD13 B LEU   A 1 164 ? 10.255 -7.760  2.178   0.30 18.32 ?  164 LEU   A HD13 1 
ATOM   3741 H  HD21 A LEU   A 1 164 ? 9.929  -8.162  -1.181  0.70 20.05 ?  164 LEU   A HD21 1 
ATOM   3742 H  HD21 B LEU   A 1 164 ? 10.016 -8.046  -0.763  0.30 18.41 ?  164 LEU   A HD21 1 
ATOM   3743 H  HD22 A LEU   A 1 164 ? 10.031 -9.412  -0.206  0.70 20.05 ?  164 LEU   A HD22 1 
ATOM   3744 H  HD22 B LEU   A 1 164 ? 10.169 -9.315  0.180   0.30 18.41 ?  164 LEU   A HD22 1 
ATOM   3745 H  HD23 A LEU   A 1 164 ? 8.803  -9.282  -1.205  0.70 20.05 ?  164 LEU   A HD23 1 
ATOM   3746 H  HD23 B LEU   A 1 164 ? 8.937  -9.211  -0.818  0.30 18.41 ?  164 LEU   A HD23 1 
ATOM   3747 N  N    A VAL   A 1 165 ? 5.546  -10.568 2.698   0.70 16.25 ?  165 VAL   A N    1 
ATOM   3748 N  N    B VAL   A 1 165 ? 5.585  -10.606 3.011   0.30 16.35 ?  165 VAL   A N    1 
ATOM   3749 C  CA   A VAL   A 1 165 ? 5.074  -11.634 3.578   0.70 16.29 ?  165 VAL   A CA   1 
ATOM   3750 C  CA   B VAL   A 1 165 ? 5.081  -11.667 3.874   0.30 16.56 ?  165 VAL   A CA   1 
ATOM   3751 C  C    A VAL   A 1 165 ? 4.056  -12.503 2.854   0.70 16.31 ?  165 VAL   A C    1 
ATOM   3752 C  C    B VAL   A 1 165 ? 4.031  -12.494 3.145   0.30 16.68 ?  165 VAL   A C    1 
ATOM   3753 O  O    A VAL   A 1 165 ? 4.177  -13.734 2.812   0.70 16.46 ?  165 VAL   A O    1 
ATOM   3754 O  O    B VAL   A 1 165 ? 4.075  -13.731 3.155   0.30 16.49 ?  165 VAL   A O    1 
ATOM   3755 C  CB   A VAL   A 1 165 ? 4.494  -11.031 4.871   0.70 17.07 ?  165 VAL   A CB   1 
ATOM   3756 C  CB   B VAL   A 1 165 ? 4.528  -11.075 5.182   0.30 16.75 ?  165 VAL   A CB   1 
ATOM   3757 C  CG1  A VAL   A 1 165 ? 3.737  -12.085 5.673   0.70 17.53 ?  165 VAL   A CG1  1 
ATOM   3758 C  CG1  B VAL   A 1 165 ? 3.862  -12.162 6.014   0.30 16.82 ?  165 VAL   A CG1  1 
ATOM   3759 C  CG2  A VAL   A 1 165 ? 5.601  -10.389 5.705   0.70 17.69 ?  165 VAL   A CG2  1 
ATOM   3760 C  CG2  B VAL   A 1 165 ? 5.636  -10.388 5.966   0.30 17.02 ?  165 VAL   A CG2  1 
ATOM   3761 H  H    A VAL   A 1 165 ? 5.335  -9.778  2.959   0.70 19.49 ?  165 VAL   A H    1 
ATOM   3762 H  H    B VAL   A 1 165 ? 5.384  -9.810  3.266   0.30 19.61 ?  165 VAL   A H    1 
ATOM   3763 H  HA   A VAL   A 1 165 ? 5.821  -12.197 3.824   0.70 19.53 ?  165 VAL   A HA   1 
ATOM   3764 H  HA   B VAL   A 1 165 ? 5.814  -12.257 4.103   0.30 19.85 ?  165 VAL   A HA   1 
ATOM   3765 H  HB   A VAL   A 1 165 ? 3.864  -10.333 4.637   0.70 20.46 ?  165 VAL   A HB   1 
ATOM   3766 H  HB   B VAL   A 1 165 ? 3.856  -10.409 4.968   0.30 20.09 ?  165 VAL   A HB   1 
ATOM   3767 H  HG11 A VAL   A 1 165 ? 3.630  -11.769 6.585   0.70 21.02 ?  165 VAL   A HG11 1 
ATOM   3768 H  HG11 B VAL   A 1 165 ? 3.748  -11.837 6.919   0.30 20.17 ?  165 VAL   A HG11 1 
ATOM   3769 H  HG12 A VAL   A 1 165 ? 2.865  -12.224 5.271   0.70 21.02 ?  165 VAL   A HG12 1 
ATOM   3770 H  HG12 B VAL   A 1 165 ? 2.997  -12.372 5.626   0.30 20.17 ?  165 VAL   A HG12 1 
ATOM   3771 H  HG13 A VAL   A 1 165 ? 4.243  -12.911 5.668   0.70 21.02 ?  165 VAL   A HG13 1 
ATOM   3772 H  HG13 B VAL   A 1 165 ? 4.428  -12.949 6.013   0.30 20.17 ?  165 VAL   A HG13 1 
ATOM   3773 H  HG21 A VAL   A 1 165 ? 5.216  -10.030 6.522   0.70 21.22 ?  165 VAL   A HG21 1 
ATOM   3774 H  HG21 B VAL   A 1 165 ? 5.260  -10.009 6.776   0.30 20.41 ?  165 VAL   A HG21 1 
ATOM   3775 H  HG22 A VAL   A 1 165 ? 6.266  -11.060 5.923   0.70 21.22 ?  165 VAL   A HG22 1 
ATOM   3776 H  HG22 B VAL   A 1 165 ? 6.316  -11.041 6.190   0.30 20.41 ?  165 VAL   A HG22 1 
ATOM   3777 H  HG23 A VAL   A 1 165 ? 6.009  -9.673  5.192   0.70 21.22 ?  165 VAL   A HG23 1 
ATOM   3778 H  HG23 B VAL   A 1 165 ? 6.021  -9.684  5.421   0.30 20.41 ?  165 VAL   A HG23 1 
ATOM   3779 N  N    A SER   A 1 166 ? 3.038  -11.872 2.267   0.70 17.02 ?  166 SER   A N    1 
ATOM   3780 N  N    B SER   A 1 166 ? 3.065  -11.825 2.509   0.30 16.93 ?  166 SER   A N    1 
ATOM   3781 C  CA   A SER   A 1 166 ? 1.929  -12.614 1.682   0.70 18.16 ?  166 SER   A CA   1 
ATOM   3782 C  CA   B SER   A 1 166 ? 1.935  -12.547 1.931   0.30 17.10 ?  166 SER   A CA   1 
ATOM   3783 C  C    A SER   A 1 166 ? 2.349  -13.413 0.461   0.70 18.96 ?  166 SER   A C    1 
ATOM   3784 C  C    B SER   A 1 166 ? 2.389  -13.540 0.866   0.30 17.72 ?  166 SER   A C    1 
ATOM   3785 O  O    A SER   A 1 166 ? 1.667  -14.381 0.106   0.70 20.38 ?  166 SER   A O    1 
ATOM   3786 O  O    B SER   A 1 166 ? 1.841  -14.646 0.767   0.30 17.86 ?  166 SER   A O    1 
ATOM   3787 C  CB   A SER   A 1 166 ? 0.804  -11.655 1.277   0.70 18.91 ?  166 SER   A CB   1 
ATOM   3788 C  CB   B SER   A 1 166 ? 0.879  -11.564 1.405   0.30 16.96 ?  166 SER   A CB   1 
ATOM   3789 O  OG   A SER   A 1 166 ? 0.210  -11.022 2.402   0.70 19.91 ?  166 SER   A OG   1 
ATOM   3790 O  OG   B SER   A 1 166 ? 1.239  -11.008 0.155   0.30 17.10 ?  166 SER   A OG   1 
ATOM   3791 H  H    A SER   A 1 166 ? 2.964  -11.023 2.196   0.70 20.41 ?  166 SER   A H    1 
ATOM   3792 H  H    B SER   A 1 166 ? 3.032  -10.969 2.412   0.30 20.30 ?  166 SER   A H    1 
ATOM   3793 H  HA   A SER   A 1 166 ? 1.564  -13.232 2.340   0.70 21.77 ?  166 SER   A HA   1 
ATOM   3794 H  HA   B SER   A 1 166 ? 1.509  -13.064 2.624   0.30 20.51 ?  166 SER   A HA   1 
ATOM   3795 H  HB2  A SER   A 1 166 ? 1.167  -10.984 0.680   0.70 22.68 ?  166 SER   A HB2  1 
ATOM   3796 H  HB2  B SER   A 1 166 ? 0.032  -12.028 1.301   0.30 20.33 ?  166 SER   A HB2  1 
ATOM   3797 H  HB3  A SER   A 1 166 ? 0.107  -12.156 0.821   0.70 22.68 ?  166 SER   A HB3  1 
ATOM   3798 H  HB3  B SER   A 1 166 ? 0.769  -10.841 2.052   0.30 20.33 ?  166 SER   A HB3  1 
ATOM   3799 H  HG   A SER   A 1 166 ? -0.380 -10.482 2.152   0.70 23.87 ?  166 SER   A HG   1 
ATOM   3800 H  HG   B SER   A 1 166 ? 1.986  -10.625 0.213   0.30 20.50 ?  166 SER   A HG   1 
ATOM   3801 N  N    A SER   A 1 167 ? 3.432  -13.018 -0.204  0.70 18.12 ?  167 SER   A N    1 
ATOM   3802 N  N    B SER   A 1 167 ? 3.416  -13.194 0.094   0.30 18.62 ?  167 SER   A N    1 
ATOM   3803 C  CA   A SER   A 1 167 ? 3.917  -13.730 -1.374  0.70 18.61 ?  167 SER   A CA   1 
ATOM   3804 C  CA   B SER   A 1 167 ? 3.923  -14.057 -0.972  0.30 19.69 ?  167 SER   A CA   1 
ATOM   3805 C  C    A SER   A 1 167 ? 5.061  -14.680 -1.052  0.70 18.48 ?  167 SER   A C    1 
ATOM   3806 C  C    B SER   A 1 167 ? 5.294  -14.574 -0.546  0.30 19.89 ?  167 SER   A C    1 
ATOM   3807 O  O    A SER   A 1 167 ? 5.562  -15.350 -1.960  0.70 18.81 ?  167 SER   A O    1 
ATOM   3808 O  O    B SER   A 1 167 ? 6.332  -14.013 -0.901  0.30 21.15 ?  167 SER   A O    1 
ATOM   3809 C  CB   A SER   A 1 167 ? 4.364  -12.736 -2.454  0.70 19.16 ?  167 SER   A CB   1 
ATOM   3810 C  CB   B SER   A 1 167 ? 3.987  -13.297 -2.307  0.30 20.46 ?  167 SER   A CB   1 
ATOM   3811 O  OG   A SER   A 1 167 ? 5.437  -11.924 -1.992  0.70 18.99 ?  167 SER   A OG   1 
ATOM   3812 O  OG   B SER   A 1 167 ? 4.709  -12.087 -2.164  0.30 21.32 ?  167 SER   A OG   1 
ATOM   3813 H  H    A SER   A 1 167 ? 3.890  -12.319 0.002   0.70 21.73 ?  167 SER   A H    1 
ATOM   3814 H  H    B SER   A 1 167 ? 3.859  -12.457 0.177   0.30 22.33 ?  167 SER   A H    1 
ATOM   3815 H  HA   A SER   A 1 167 ? 3.188  -14.251 -1.742  0.70 22.31 ?  167 SER   A HA   1 
ATOM   3816 H  HA   B SER   A 1 167 ? 3.330  -14.813 -1.085  0.30 23.61 ?  167 SER   A HA   1 
ATOM   3817 H  HB2  A SER   A 1 167 ? 4.664  -13.234 -3.231  0.70 22.98 ?  167 SER   A HB2  1 
ATOM   3818 H  HB2  B SER   A 1 167 ? 4.436  -13.853 -2.966  0.30 24.54 ?  167 SER   A HB2  1 
ATOM   3819 H  HB3  A SER   A 1 167 ? 3.610  -12.173 -2.697  0.70 22.98 ?  167 SER   A HB3  1 
ATOM   3820 H  HB3  B SER   A 1 167 ? 3.084  -13.100 -2.605  0.30 24.54 ?  167 SER   A HB3  1 
ATOM   3821 H  HG   A SER   A 1 167 ? 5.175  -11.476 -1.323  0.70 22.77 ?  167 SER   A HG   1 
ATOM   3822 H  HG   B SER   A 1 167 ? 4.316  -11.582 -1.617  0.30 25.56 ?  167 SER   A HG   1 
ATOM   3823 N  N    A PHE   A 1 168 ? 5.491  -14.755 0.208   0.70 17.88 ?  168 PHE   A N    1 
ATOM   3824 N  N    B PHE   A 1 168 ? 5.294  -15.660 0.230   0.30 18.44 ?  168 PHE   A N    1 
ATOM   3825 C  CA   A PHE   A 1 168 ? 6.670  -15.548 0.522   0.70 18.37 ?  168 PHE   A CA   1 
ATOM   3826 C  CA   B PHE   A 1 168 ? 6.554  -16.276 0.636   0.30 17.56 ?  168 PHE   A CA   1 
ATOM   3827 C  C    A PHE   A 1 168 ? 6.366  -17.031 0.403   0.70 20.17 ?  168 PHE   A C    1 
ATOM   3828 C  C    B PHE   A 1 168 ? 6.535  -17.798 0.563   0.30 17.85 ?  168 PHE   A C    1 
ATOM   3829 O  O    A PHE   A 1 168 ? 5.372  -17.522 0.949   0.70 21.75 ?  168 PHE   A O    1 
ATOM   3830 O  O    B PHE   A 1 168 ? 7.408  -18.391 -0.077  0.30 17.29 ?  168 PHE   A O    1 
ATOM   3831 C  CB   A PHE   A 1 168 ? 7.193  -15.259 1.925   0.70 17.90 ?  168 PHE   A CB   1 
ATOM   3832 C  CB   B PHE   A 1 168 ? 6.969  -15.834 2.040   0.30 17.49 ?  168 PHE   A CB   1 
ATOM   3833 C  CG   A PHE   A 1 168 ? 8.453  -16.014 2.239   0.70 17.23 ?  168 PHE   A CG   1 
ATOM   3834 C  CG   B PHE   A 1 168 ? 8.319  -16.355 2.457   0.30 17.16 ?  168 PHE   A CG   1 
ATOM   3835 C  CD1  A PHE   A 1 168 ? 9.636  -15.678 1.606   0.70 17.36 ?  168 PHE   A CD1  1 
ATOM   3836 C  CD1  B PHE   A 1 168 ? 9.476  -15.818 1.918   0.30 17.23 ?  168 PHE   A CD1  1 
ATOM   3837 C  CD2  A PHE   A 1 168 ? 8.455  -17.086 3.118   0.70 16.87 ?  168 PHE   A CD2  1 
ATOM   3838 C  CD2  B PHE   A 1 168 ? 8.432  -17.384 3.378   0.30 17.24 ?  168 PHE   A CD2  1 
ATOM   3839 C  CE1  A PHE   A 1 168 ? 10.799 -16.378 1.863   0.70 16.64 ?  168 PHE   A CE1  1 
ATOM   3840 C  CE1  B PHE   A 1 168 ? 10.719 -16.292 2.292   0.30 17.30 ?  168 PHE   A CE1  1 
ATOM   3841 C  CE2  A PHE   A 1 168 ? 9.623  -17.786 3.380   0.70 16.96 ?  168 PHE   A CE2  1 
ATOM   3842 C  CE2  B PHE   A 1 168 ? 9.676  -17.861 3.757   0.30 17.35 ?  168 PHE   A CE2  1 
ATOM   3843 C  CZ   A PHE   A 1 168 ? 10.792 -17.428 2.751   0.70 16.62 ?  168 PHE   A CZ   1 
ATOM   3844 C  CZ   B PHE   A 1 168 ? 10.819 -17.314 3.213   0.30 17.32 ?  168 PHE   A CZ   1 
ATOM   3845 H  H    A PHE   A 1 168 ? 5.127  -14.361 0.881   0.70 21.44 ?  168 PHE   A H    1 
ATOM   3846 H  H    B PHE   A 1 168 ? 4.588  -16.051 0.525   0.30 22.11 ?  168 PHE   A H    1 
ATOM   3847 H  HA   A PHE   A 1 168 ? 7.370  -15.331 -0.112  0.70 22.02 ?  168 PHE   A HA   1 
ATOM   3848 H  HA   B PHE   A 1 168 ? 7.245  -15.982 0.027   0.30 21.06 ?  168 PHE   A HA   1 
ATOM   3849 H  HB2  A PHE   A 1 168 ? 7.382  -14.311 2.001   0.70 21.46 ?  168 PHE   A HB2  1 
ATOM   3850 H  HB2  B PHE   A 1 168 ? 7.006  -14.867 2.062   0.30 20.98 ?  168 PHE   A HB2  1 
ATOM   3851 H  HB3  A PHE   A 1 168 ? 6.518  -15.517 2.573   0.70 21.46 ?  168 PHE   A HB3  1 
ATOM   3852 H  HB3  B PHE   A 1 168 ? 6.317  -16.158 2.678   0.30 20.98 ?  168 PHE   A HB3  1 
ATOM   3853 H  HD1  A PHE   A 1 168 ? 9.653  -14.968 1.005   0.70 20.82 ?  168 PHE   A HD1  1 
ATOM   3854 H  HD1  B PHE   A 1 168 ? 9.418  -15.130 1.296   0.30 20.65 ?  168 PHE   A HD1  1 
ATOM   3855 H  HD2  A PHE   A 1 168 ? 7.666  -17.330 3.546   0.70 20.23 ?  168 PHE   A HD2  1 
ATOM   3856 H  HD2  B PHE   A 1 168 ? 7.665  -17.758 3.748   0.30 20.67 ?  168 PHE   A HD2  1 
ATOM   3857 H  HE1  A PHE   A 1 168 ? 11.595 -16.138 1.440   0.70 19.95 ?  168 PHE   A HE1  1 
ATOM   3858 H  HE1  B PHE   A 1 168 ? 11.490 -15.922 1.924   0.30 20.74 ?  168 PHE   A HE1  1 
ATOM   3859 H  HE2  A PHE   A 1 168 ? 9.614  -18.499 3.979   0.70 20.34 ?  168 PHE   A HE2  1 
ATOM   3860 H  HE2  B PHE   A 1 168 ? 9.739  -18.551 4.378   0.30 20.80 ?  168 PHE   A HE2  1 
ATOM   3861 H  HZ   A PHE   A 1 168 ? 11.579 -17.898 2.924   0.70 19.93 ?  168 PHE   A HZ   1 
ATOM   3862 H  HZ   B PHE   A 1 168 ? 11.656 -17.633 3.466   0.30 20.77 ?  168 PHE   A HZ   1 
ATOM   3863 N  N    A LEU   A 1 169 ? 7.250  -17.753 -0.278  0.70 21.58 ?  169 LEU   A N    1 
ATOM   3864 N  N    B LEU   A 1 169 ? 5.580  -18.441 1.226   0.30 18.60 ?  169 LEU   A N    1 
ATOM   3865 C  CA   A LEU   A 1 169 ? 7.069  -19.184 -0.450  0.70 23.95 ?  169 LEU   A CA   1 
ATOM   3866 C  CA   B LEU   A 1 169 ? 5.574  -19.901 1.298   0.30 19.81 ?  169 LEU   A CA   1 
ATOM   3867 C  C    A LEU   A 1 169 ? 7.896  -19.943 0.576   0.70 24.12 ?  169 LEU   A C    1 
ATOM   3868 C  C    B LEU   A 1 169 ? 4.974  -20.525 0.042   0.30 20.74 ?  169 LEU   A C    1 
ATOM   3869 O  O    A LEU   A 1 169 ? 7.330  -20.455 1.546   0.70 24.53 ?  169 LEU   A O    1 
ATOM   3870 O  O    B LEU   A 1 169 ? 5.366  -21.621 -0.361  0.30 21.50 ?  169 LEU   A O    1 
ATOM   3871 C  CB   A LEU   A 1 169 ? 7.417  -19.609 -1.880  0.70 25.14 ?  169 LEU   A CB   1 
ATOM   3872 C  CB   B LEU   A 1 169 ? 4.812  -20.382 2.537   0.30 19.96 ?  169 LEU   A CB   1 
ATOM   3873 C  CG   A LEU   A 1 169 ? 7.091  -21.062 -2.245  0.70 26.29 ?  169 LEU   A CG   1 
ATOM   3874 C  CG   B LEU   A 1 169 ? 5.029  -21.849 2.923   0.30 19.98 ?  169 LEU   A CG   1 
ATOM   3875 C  CD1  A LEU   A 1 169 ? 5.662  -21.415 -1.866  0.70 26.68 ?  169 LEU   A CD1  1 
ATOM   3876 C  CD1  B LEU   A 1 169 ? 6.489  -22.087 3.276   0.30 20.43 ?  169 LEU   A CD1  1 
ATOM   3877 C  CD2  A LEU   A 1 169 ? 7.321  -21.313 -3.729  0.70 26.54 ?  169 LEU   A CD2  1 
ATOM   3878 C  CD2  B LEU   A 1 169 ? 4.123  -22.253 4.078   0.30 20.04 ?  169 LEU   A CD2  1 
ATOM   3879 O  OXT  A LEU   A 1 169 ? 9.120  -20.051 0.479   0.70 23.45 -1 169 LEU   A OXT  1 
ATOM   3880 O  OXT  B LEU   A 1 169 ? 4.086  -19.957 -0.595  0.30 20.90 -1 169 LEU   A OXT  1 
ATOM   3881 H  H    A LEU   A 1 169 ? 7.966  -17.439 -0.645  0.70 25.88 ?  169 LEU   A H    1 
ATOM   3882 H  H    B LEU   A 1 169 ? 4.930  -18.063 1.640   0.30 22.30 ?  169 LEU   A H    1 
ATOM   3883 H  HA   A LEU   A 1 169 ? 6.149  -19.407 -0.280  0.70 28.72 ?  169 LEU   A HA   1 
ATOM   3884 H  HA   B LEU   A 1 169 ? 6.490  -20.206 1.372   0.30 23.76 ?  169 LEU   A HA   1 
ATOM   3885 H  HB2  A LEU   A 1 169 ? 6.921  -19.043 -2.493  0.70 30.15 ?  169 LEU   A HB2  1 
ATOM   3886 H  HB2  B LEU   A 1 169 ? 5.088  -19.843 3.293   0.30 23.94 ?  169 LEU   A HB2  1 
ATOM   3887 H  HB3  A LEU   A 1 169 ? 8.366  -19.484 -2.021  0.70 30.15 ?  169 LEU   A HB3  1 
ATOM   3888 H  HB3  B LEU   A 1 169 ? 3.864  -20.264 2.381   0.30 23.94 ?  169 LEU   A HB3  1 
ATOM   3889 H  HG   A LEU   A 1 169 ? 7.683  -21.651 -1.752  0.70 31.54 ?  169 LEU   A HG   1 
ATOM   3890 H  HG   B LEU   A 1 169 ? 4.812  -22.412 2.164   0.30 23.96 ?  169 LEU   A HG   1 
ATOM   3891 H  HD11 A LEU   A 1 169 ? 5.417  -22.249 -2.296  0.70 31.99 ?  169 LEU   A HD11 1 
ATOM   3892 H  HD11 B LEU   A 1 169 ? 6.571  -22.945 3.720   0.30 24.50 ?  169 LEU   A HD11 1 
ATOM   3893 H  HD12 A LEU   A 1 169 ? 5.605  -21.513 -0.902  0.70 31.99 ?  169 LEU   A HD12 1 
ATOM   3894 H  HD12 B LEU   A 1 169 ? 7.017  -22.085 2.462   0.30 24.50 ?  169 LEU   A HD12 1 
ATOM   3895 H  HD13 A LEU   A 1 169 ? 5.071  -20.705 -2.163  0.70 31.99 ?  169 LEU   A HD13 1 
ATOM   3896 H  HD13 B LEU   A 1 169 ? 6.790  -21.379 3.869   0.30 24.50 ?  169 LEU   A HD13 1 
ATOM   3897 H  HD21 A LEU   A 1 169 ? 7.117  -22.241 -3.929  0.70 31.84 ?  169 LEU   A HD21 1 
ATOM   3898 H  HD21 B LEU   A 1 169 ? 4.282  -23.185 4.294   0.30 24.03 ?  169 LEU   A HD21 1 
ATOM   3899 H  HD22 A LEU   A 1 169 ? 6.738  -20.730 -4.242  0.70 31.84 ?  169 LEU   A HD22 1 
ATOM   3900 H  HD22 B LEU   A 1 169 ? 4.327  -21.696 4.847   0.30 24.03 ?  169 LEU   A HD22 1 
ATOM   3901 H  HD23 A LEU   A 1 169 ? 8.248  -21.126 -3.942  0.70 31.84 ?  169 LEU   A HD23 1 
ATOM   3902 H  HD23 B LEU   A 1 169 ? 3.200  -22.126 3.813   0.30 24.03 ?  169 LEU   A HD23 1 
ATOM   3903 N  N    A SER   B 1 1   ? 50.841 -9.277  -23.730 0.70 27.76 ?  1   SER   B N    1 
ATOM   3904 N  N    B SER   B 1 1   ? 50.781 -9.260  -23.694 0.30 26.82 ?  1   SER   B N    1 
ATOM   3905 C  CA   A SER   B 1 1   ? 51.320 -10.318 -22.799 0.70 28.10 ?  1   SER   B CA   1 
ATOM   3906 C  CA   B SER   B 1 1   ? 51.278 -10.265 -22.731 0.30 26.87 ?  1   SER   B CA   1 
ATOM   3907 C  C    A SER   B 1 1   ? 50.238 -11.359 -22.544 0.70 27.09 ?  1   SER   B C    1 
ATOM   3908 C  C    B SER   B 1 1   ? 50.232 -11.343 -22.511 0.30 26.16 ?  1   SER   B C    1 
ATOM   3909 O  O    A SER   B 1 1   ? 49.049 -11.151 -22.828 0.70 26.84 ?  1   SER   B O    1 
ATOM   3910 O  O    B SER   B 1 1   ? 49.046 -11.156 -22.798 0.30 26.03 ?  1   SER   B O    1 
ATOM   3911 C  CB   A SER   B 1 1   ? 51.764 -9.700  -21.476 0.70 28.73 ?  1   SER   B CB   1 
ATOM   3912 C  CB   B SER   B 1 1   ? 51.629 -9.610  -21.399 0.30 27.21 ?  1   SER   B CB   1 
ATOM   3913 O  OG   A SER   B 1 1   ? 50.648 -9.409  -20.657 0.70 30.66 ?  1   SER   B OG   1 
ATOM   3914 O  OG   B SER   B 1 1   ? 50.462 -9.370  -20.635 0.30 28.15 ?  1   SER   B OG   1 
ATOM   3915 H  H1   A SER   B 1 1   ? 50.757 -9.631  -24.540 0.70 33.30 ?  1   SER   B H1   1 
ATOM   3916 H  H1   B SER   B 1 1   ? 50.738 -9.629  -24.500 0.30 32.17 ?  1   SER   B H1   1 
ATOM   3917 H  H2   A SER   B 1 1   ? 50.059 -8.975  -23.448 0.70 33.30 ?  1   SER   B H2   1 
ATOM   3918 H  H2   B SER   B 1 1   ? 49.976 -8.990  -23.441 0.30 32.17 ?  1   SER   B H2   1 
ATOM   3919 H  H3   A SER   B 1 1   ? 51.434 -8.615  -23.751 0.70 33.30 ?  1   SER   B H3   1 
ATOM   3920 H  H3   B SER   B 1 1   ? 51.343 -8.573  -23.706 0.30 32.17 ?  1   SER   B H3   1 
ATOM   3921 H  HA   A SER   B 1 1   ? 52.083 -10.756 -23.203 0.70 33.70 ?  1   SER   B HA   1 
ATOM   3922 H  HA   B SER   B 1 1   ? 52.073 -10.673 -23.097 0.30 32.22 ?  1   SER   B HA   1 
ATOM   3923 H  HB2  A SER   B 1 1   ? 52.334 -10.333 -21.016 0.70 34.46 ?  1   SER   B HB2  1 
ATOM   3924 H  HB2  B SER   B 1 1   ? 52.221 -10.203 -20.912 0.30 32.63 ?  1   SER   B HB2  1 
ATOM   3925 H  HB3  A SER   B 1 1   ? 52.254 -8.881  -21.657 0.70 34.46 ?  1   SER   B HB3  1 
ATOM   3926 H  HB3  B SER   B 1 1   ? 52.071 -8.764  -21.569 0.30 32.63 ?  1   SER   B HB3  1 
ATOM   3927 H  HG   A SER   B 1 1   ? 50.895 -8.948  -19.998 0.70 36.78 ?  1   SER   B HG   1 
ATOM   3928 H  HG   B SER   B 1 1   ? 50.639 -8.845  -20.005 0.30 33.77 ?  1   SER   B HG   1 
ATOM   3929 N  N    A MET   B 1 2   ? 50.672 -12.482 -21.993 0.70 26.31 ?  2   MET   B N    1 
ATOM   3930 N  N    B MET   B 1 2   ? 50.685 -12.474 -21.987 0.30 25.45 ?  2   MET   B N    1 
ATOM   3931 C  CA   A MET   B 1 2   ? 49.842 -13.668 -21.833 0.70 26.28 ?  2   MET   B CA   1 
ATOM   3932 C  CA   B MET   B 1 2   ? 49.854 -13.656 -21.810 0.30 24.97 ?  2   MET   B CA   1 
ATOM   3933 C  C    A MET   B 1 2   ? 49.586 -13.875 -20.347 0.70 24.08 ?  2   MET   B C    1 
ATOM   3934 C  C    B MET   B 1 2   ? 49.595 -13.831 -20.324 0.30 23.49 ?  2   MET   B C    1 
ATOM   3935 O  O    A MET   B 1 2   ? 50.512 -14.175 -19.587 0.70 24.39 ?  2   MET   B O    1 
ATOM   3936 O  O    B MET   B 1 2   ? 50.526 -14.066 -19.546 0.30 23.61 ?  2   MET   B O    1 
ATOM   3937 C  CB   A MET   B 1 2   ? 50.569 -14.862 -22.438 0.70 29.93 ?  2   MET   B CB   1 
ATOM   3938 C  CB   B MET   B 1 2   ? 50.577 -14.863 -22.380 0.30 26.59 ?  2   MET   B CB   1 
ATOM   3939 C  CG   A MET   B 1 2   ? 49.721 -16.106 -22.614 0.70 33.28 ?  2   MET   B CG   1 
ATOM   3940 C  CG   B MET   B 1 2   ? 49.677 -16.024 -22.775 0.30 27.94 ?  2   MET   B CG   1 
ATOM   3941 S  SD   A MET   B 1 2   ? 50.577 -17.334 -23.617 0.70 36.63 ?  2   MET   B SD   1 
ATOM   3942 S  SD   B MET   B 1 2   ? 50.540 -17.151 -23.873 0.30 29.13 ?  2   MET   B SD   1 
ATOM   3943 C  CE   A MET   B 1 2   ? 51.123 -16.296 -24.967 0.70 36.87 ?  2   MET   B CE   1 
ATOM   3944 C  CE   B MET   B 1 2   ? 51.534 -15.986 -24.785 0.30 29.47 ?  2   MET   B CE   1 
ATOM   3945 H  H    A MET   B 1 2   ? 51.473 -12.589 -21.696 0.70 31.56 ?  2   MET   B H    1 
ATOM   3946 H  H    B MET   B 1 2   ? 51.496 -12.591 -21.722 0.30 30.53 ?  2   MET   B H    1 
ATOM   3947 H  HA   A MET   B 1 2   ? 49.004 -13.552 -22.306 0.70 31.52 ?  2   MET   B HA   1 
ATOM   3948 H  HA   B MET   B 1 2   ? 49.021 -13.556 -22.295 0.30 29.94 ?  2   MET   B HA   1 
ATOM   3949 H  HB2  A MET   B 1 2   ? 50.897 -14.578 -23.302 0.70 35.91 ?  2   MET   B HB2  1 
ATOM   3950 H  HB2  B MET   B 1 2   ? 51.038 -14.505 -23.145 0.30 31.89 ?  2   MET   B HB2  1 
ATOM   3951 H  HB3  A MET   B 1 2   ? 51.315 -15.107 -21.874 0.70 35.91 ?  2   MET   B HB3  1 
ATOM   3952 H  HB3  B MET   B 1 2   ? 51.219 -15.212 -21.748 0.30 31.89 ?  2   MET   B HB3  1 
ATOM   3953 H  HG2  A MET   B 1 2   ? 49.537 -16.494 -21.741 0.70 39.92 ?  2   MET   B HG2  1 
ATOM   3954 H  HG2  B MET   B 1 2   ? 49.410 -16.516 -21.976 0.30 33.51 ?  2   MET   B HG2  1 
ATOM   3955 H  HG3  A MET   B 1 2   ? 48.893 -15.877 -23.063 0.70 39.92 ?  2   MET   B HG3  1 
ATOM   3956 H  HG3  B MET   B 1 2   ? 48.895 -15.699 -23.242 0.30 33.51 ?  2   MET   B HG3  1 
ATOM   3957 H  HE1  A MET   B 1 2   ? 51.285 -16.849 -25.735 0.70 44.22 ?  2   MET   B HE1  1 
ATOM   3958 H  HE1  B MET   B 1 2   ? 51.845 -16.437 -25.553 0.30 35.35 ?  2   MET   B HE1  1 
ATOM   3959 H  HE2  A MET   B 1 2   ? 50.424 -15.647 -25.160 0.70 44.22 ?  2   MET   B HE2  1 
ATOM   3960 H  HE2  B MET   B 1 2   ? 50.980 -15.224 -25.045 0.30 35.35 ?  2   MET   B HE2  1 
ATOM   3961 H  HE3  A MET   B 1 2   ? 51.939 -15.832 -24.708 0.70 44.22 ?  2   MET   B HE3  1 
ATOM   3962 H  HE3  B MET   B 1 2   ? 52.291 -15.690 -24.240 0.30 35.35 ?  2   MET   B HE3  1 
ATOM   3963 N  N    . VAL   B 1 3   ? 48.333 -13.699 -19.933 1.00 22.16 ?  3   VAL   B N    1 
ATOM   3964 C  CA   . VAL   B 1 3   ? 47.918 -13.928 -18.559 1.00 20.71 ?  3   VAL   B CA   1 
ATOM   3965 C  C    . VAL   B 1 3   ? 46.681 -14.814 -18.581 1.00 18.81 ?  3   VAL   B C    1 
ATOM   3966 O  O    . VAL   B 1 3   ? 45.943 -14.871 -19.568 1.00 19.46 ?  3   VAL   B O    1 
ATOM   3967 C  CB   . VAL   B 1 3   ? 47.641 -12.612 -17.798 1.00 22.12 ?  3   VAL   B CB   1 
ATOM   3968 C  CG1  . VAL   B 1 3   ? 48.922 -11.770 -17.683 1.00 22.81 ?  3   VAL   B CG1  1 
ATOM   3969 C  CG2  . VAL   B 1 3   ? 46.529 -11.827 -18.477 1.00 22.80 ?  3   VAL   B CG2  1 
ATOM   3970 H  H    A VAL   B 1 3   ? 47.694 -13.452 -20.454 0.70 26.58 ?  3   VAL   B H    1 
ATOM   3971 H  H    B VAL   B 1 3   ? 47.692 -13.471 -20.461 0.30 26.58 ?  3   VAL   B H    1 
ATOM   3972 H  HA   . VAL   B 1 3   ? 48.619 -14.405 -18.089 1.00 24.83 ?  3   VAL   B HA   1 
ATOM   3973 H  HB   . VAL   B 1 3   ? 47.350 -12.829 -16.901 1.00 26.53 ?  3   VAL   B HB   1 
ATOM   3974 H  HG11 . VAL   B 1 3   ? 48.718 -10.956 -17.196 1.00 27.35 ?  3   VAL   B HG11 1 
ATOM   3975 H  HG12 . VAL   B 1 3   ? 49.593 -12.283 -17.205 1.00 27.35 ?  3   VAL   B HG12 1 
ATOM   3976 H  HG13 . VAL   B 1 3   ? 49.239 -11.555 -18.573 1.00 27.35 ?  3   VAL   B HG13 1 
ATOM   3977 H  HG21 . VAL   B 1 3   ? 46.467 -10.953 -18.066 1.00 27.35 ?  3   VAL   B HG21 1 
ATOM   3978 H  HG22 . VAL   B 1 3   ? 46.736 -11.736 -19.420 1.00 27.35 ?  3   VAL   B HG22 1 
ATOM   3979 H  HG23 . VAL   B 1 3   ? 45.693 -12.306 -18.367 1.00 27.35 ?  3   VAL   B HG23 1 
ATOM   3980 N  N    . ASN   B 1 4   ? 46.466 -15.520 -17.476 1.00 16.93 ?  4   ASN   B N    1 
ATOM   3981 C  CA   . ASN   B 1 4   ? 45.324 -16.426 -17.357 1.00 15.95 ?  4   ASN   B CA   1 
ATOM   3982 C  C    . ASN   B 1 4   ? 45.262 -17.391 -18.539 1.00 16.34 ?  4   ASN   B C    1 
ATOM   3983 O  O    . ASN   B 1 4   ? 44.199 -17.643 -19.103 1.00 17.07 ?  4   ASN   B O    1 
ATOM   3984 C  CB   . ASN   B 1 4   ? 44.011 -15.653 -17.200 1.00 15.36 ?  4   ASN   B CB   1 
ATOM   3985 C  CG   . ASN   B 1 4   ? 43.967 -14.843 -15.915 1.00 14.88 ?  4   ASN   B CG   1 
ATOM   3986 O  OD1  . ASN   B 1 4   ? 44.248 -15.354 -14.833 1.00 14.84 ?  4   ASN   B OD1  1 
ATOM   3987 N  ND2  . ASN   B 1 4   ? 43.619 -13.568 -16.034 1.00 15.99 ?  4   ASN   B ND2  1 
ATOM   3988 H  H    . ASN   B 1 4   ? 46.971 -15.505 -16.782 1.00 20.30 ?  4   ASN   B H    1 
ATOM   3989 H  HA   . ASN   B 1 4   ? 45.444 -16.962 -16.558 1.00 19.13 ?  4   ASN   B HA   1 
ATOM   3990 H  HB2  . ASN   B 1 4   ? 43.915 -15.041 -17.949 1.00 18.42 ?  4   ASN   B HB2  1 
ATOM   3991 H  HB3  . ASN   B 1 4   ? 43.274 -16.282 -17.189 1.00 18.42 ?  4   ASN   B HB3  1 
ATOM   3992 H  HD21 . ASN   B 1 4   ? 43.585 -13.066 -15.335 1.00 19.18 ?  4   ASN   B HD21 1 
ATOM   3993 H  HD22 . ASN   B 1 4   ? 43.434 -13.238 -16.807 1.00 19.18 ?  4   ASN   B HD22 1 
ATOM   3994 N  N    . SER   B 1 5   ? 46.418 -17.934 -18.924 1.00 17.39 ?  5   SER   B N    1 
ATOM   3995 C  CA   . SER   B 1 5   ? 46.506 -18.852 -20.059 1.00 19.81 ?  5   SER   B CA   1 
ATOM   3996 C  C    . SER   B 1 5   ? 46.490 -20.271 -19.505 1.00 21.46 ?  5   SER   B C    1 
ATOM   3997 O  O    . SER   B 1 5   ? 47.514 -20.942 -19.402 1.00 23.60 ?  5   SER   B O    1 
ATOM   3998 C  CB   . SER   B 1 5   ? 47.760 -18.569 -20.884 1.00 21.60 ?  5   SER   B CB   1 
ATOM   3999 O  OG   . SER   B 1 5   ? 48.932 -18.763 -20.113 1.00 24.40 ?  5   SER   B OG   1 
ATOM   4000 H  H    . SER   B 1 5   ? 47.174 -17.789 -18.538 1.00 20.85 ?  5   SER   B H    1 
ATOM   4001 H  HA   . SER   B 1 5   ? 45.733 -18.734 -20.631 1.00 23.76 ?  5   SER   B HA   1 
ATOM   4002 H  HB2  . SER   B 1 5   ? 47.774 -19.165 -21.652 1.00 25.90 ?  5   SER   B HB2  1 
ATOM   4003 H  HB3  . SER   B 1 5   ? 47.724 -17.648 -21.188 1.00 25.90 ?  5   SER   B HB3  1 
ATOM   4004 H  HG   . SER   B 1 5   ? 48.986 -19.567 -19.877 1.00 29.26 ?  5   SER   B HG   1 
ATOM   4005 N  N    . PHE   B 1 6   ? 45.298 -20.713 -19.116 1.00 22.37 ?  6   PHE   B N    1 
ATOM   4006 C  CA   . PHE   B 1 6   ? 45.113 -22.054 -18.582 1.00 22.27 ?  6   PHE   B CA   1 
ATOM   4007 C  C    . PHE   B 1 6   ? 45.031 -23.046 -19.733 1.00 26.12 ?  6   PHE   B C    1 
ATOM   4008 O  O    . PHE   B 1 6   ? 44.341 -22.797 -20.726 1.00 28.30 ?  6   PHE   B O    1 
ATOM   4009 C  CB   . PHE   B 1 6   ? 43.832 -22.112 -17.751 1.00 19.99 ?  6   PHE   B CB   1 
ATOM   4010 C  CG   . PHE   B 1 6   ? 43.860 -21.246 -16.524 1.00 17.81 ?  6   PHE   B CG   1 
ATOM   4011 C  CD1  . PHE   B 1 6   ? 44.371 -21.727 -15.332 1.00 16.93 ?  6   PHE   B CD1  1 
ATOM   4012 C  CD2  . PHE   B 1 6   ? 43.372 -19.949 -16.565 1.00 16.84 ?  6   PHE   B CD2  1 
ATOM   4013 C  CE1  . PHE   B 1 6   ? 44.386 -20.931 -14.197 1.00 16.24 ?  6   PHE   B CE1  1 
ATOM   4014 C  CE2  . PHE   B 1 6   ? 43.392 -19.143 -15.440 1.00 17.59 ?  6   PHE   B CE2  1 
ATOM   4015 C  CZ   . PHE   B 1 6   ? 43.904 -19.627 -14.257 1.00 16.55 ?  6   PHE   B CZ   1 
ATOM   4016 H  H    . PHE   B 1 6   ? 44.574 -20.250 -19.153 1.00 26.83 ?  6   PHE   B H    1 
ATOM   4017 H  HA   . PHE   B 1 6   ? 45.862 -22.292 -18.018 1.00 26.70 ?  6   PHE   B HA   1 
ATOM   4018 H  HB2  . PHE   B 1 6   ? 43.088 -21.821 -18.302 1.00 23.97 ?  6   PHE   B HB2  1 
ATOM   4019 H  HB3  . PHE   B 1 6   ? 43.687 -23.028 -17.464 1.00 23.97 ?  6   PHE   B HB3  1 
ATOM   4020 H  HD1  . PHE   B 1 6   ? 44.705 -22.595 -15.288 1.00 20.30 ?  6   PHE   B HD1  1 
ATOM   4021 H  HD2  . PHE   B 1 6   ? 43.026 -19.620 -17.359 1.00 20.19 ?  6   PHE   B HD2  1 
ATOM   4022 H  HE1  . PHE   B 1 6   ? 44.743 -21.255 -13.401 1.00 19.47 ?  6   PHE   B HE1  1 
ATOM   4023 H  HE2  . PHE   B 1 6   ? 43.059 -18.276 -15.483 1.00 21.09 ?  6   PHE   B HE2  1 
ATOM   4024 H  HZ   . PHE   B 1 6   ? 43.918 -19.090 -13.498 1.00 19.85 ?  6   PHE   B HZ   1 
ATOM   4025 N  N    . SER   B 1 7   ? 45.749 -24.161 -19.605 1.00 27.66 ?  7   SER   B N    1 
ATOM   4026 C  CA   . SER   B 1 7   ? 45.833 -25.150 -20.669 1.00 30.84 ?  7   SER   B CA   1 
ATOM   4027 C  C    . SER   B 1 7   ? 45.761 -26.551 -20.082 1.00 29.26 ?  7   SER   B C    1 
ATOM   4028 O  O    . SER   B 1 7   ? 46.358 -26.831 -19.039 1.00 29.87 ?  7   SER   B O    1 
ATOM   4029 C  CB   . SER   B 1 7   ? 47.137 -24.990 -21.464 1.00 34.95 ?  7   SER   B CB   1 
ATOM   4030 O  OG   . SER   B 1 7   ? 47.152 -25.840 -22.597 1.00 37.09 ?  7   SER   B OG   1 
ATOM   4031 H  H    . SER   B 1 7   ? 46.209 -24.362 -18.904 1.00 33.17 ?  7   SER   B H    1 
ATOM   4032 H  HA   . SER   B 1 7   ? 45.089 -25.036 -21.277 1.00 36.99 ?  7   SER   B HA   1 
ATOM   4033 H  HB2  . SER   B 1 7   ? 47.215 -24.068 -21.759 1.00 41.92 ?  7   SER   B HB2  1 
ATOM   4034 H  HB3  . SER   B 1 7   ? 47.887 -25.217 -20.891 1.00 41.92 ?  7   SER   B HB3  1 
ATOM   4035 H  HG   . SER   B 1 7   ? 47.870 -25.738 -23.022 1.00 44.49 ?  7   SER   B HG   1 
ATOM   4036 N  N    . GLY   B 1 8   ? 45.028 -27.429 -20.764 1.00 28.56 ?  8   GLY   B N    1 
ATOM   4037 C  CA   . GLY   B 1 8   ? 44.977 -28.822 -20.381 1.00 27.56 ?  8   GLY   B CA   1 
ATOM   4038 C  C    . GLY   B 1 8   ? 44.038 -29.144 -19.248 1.00 25.86 ?  8   GLY   B C    1 
ATOM   4039 O  O    . GLY   B 1 8   ? 44.178 -30.206 -18.629 1.00 27.13 ?  8   GLY   B O    1 
ATOM   4040 H  H    . GLY   B 1 8   ? 44.556 -27.231 -21.454 1.00 34.25 ?  8   GLY   B H    1 
ATOM   4041 H  HA2  . GLY   B 1 8   ? 44.702 -29.346 -21.145 1.00 33.05 ?  8   GLY   B HA2  1 
ATOM   4042 H  HA3  . GLY   B 1 8   ? 45.863 -29.108 -20.117 1.00 33.05 ?  8   GLY   B HA3  1 
ATOM   4043 N  N    . TYR   B 1 9   ? 43.064 -28.282 -18.968 1.00 23.76 ?  9   TYR   B N    1 
ATOM   4044 C  CA   . TYR   B 1 9   ? 42.113 -28.554 -17.903 1.00 21.46 ?  9   TYR   B CA   1 
ATOM   4045 C  C    . TYR   B 1 9   ? 40.930 -29.351 -18.419 1.00 21.03 ?  9   TYR   B C    1 
ATOM   4046 O  O    . TYR   B 1 9   ? 40.515 -29.222 -19.575 1.00 22.81 ?  9   TYR   B O    1 
ATOM   4047 C  CB   . TYR   B 1 9   ? 41.606 -27.269 -17.256 1.00 20.56 ?  9   TYR   B CB   1 
ATOM   4048 C  CG   . TYR   B 1 9   ? 42.635 -26.645 -16.347 1.00 19.89 ?  9   TYR   B CG   1 
ATOM   4049 C  CD1  . TYR   B 1 9   ? 43.725 -25.968 -16.871 1.00 20.16 ?  9   TYR   B CD1  1 
ATOM   4050 C  CD2  . TYR   B 1 9   ? 42.531 -26.752 -14.969 1.00 19.31 ?  9   TYR   B CD2  1 
ATOM   4051 C  CE1  . TYR   B 1 9   ? 44.681 -25.411 -16.050 1.00 20.36 ?  9   TYR   B CE1  1 
ATOM   4052 C  CE2  . TYR   B 1 9   ? 43.485 -26.191 -14.136 1.00 19.53 ?  9   TYR   B CE2  1 
ATOM   4053 C  CZ   . TYR   B 1 9   ? 44.559 -25.518 -14.686 1.00 20.18 ?  9   TYR   B CZ   1 
ATOM   4054 O  OH   . TYR   B 1 9   ? 45.517 -24.967 -13.871 1.00 20.82 ?  9   TYR   B OH   1 
ATOM   4055 H  H    . TYR   B 1 9   ? 42.914 -27.549 -19.392 1.00 28.50 ?  9   TYR   B H    1 
ATOM   4056 H  HA   . TYR   B 1 9   ? 42.538 -29.082 -17.216 1.00 25.74 ?  9   TYR   B HA   1 
ATOM   4057 H  HB2  . TYR   B 1 9   ? 41.374 -26.622 -17.943 1.00 24.66 ?  9   TYR   B HB2  1 
ATOM   4058 H  HB3  . TYR   B 1 9   ? 40.828 -27.481 -16.721 1.00 24.66 ?  9   TYR   B HB3  1 
ATOM   4059 H  HD1  . TYR   B 1 9   ? 43.810 -25.895 -17.795 1.00 24.18 ?  9   TYR   B HD1  1 
ATOM   4060 H  HD2  . TYR   B 1 9   ? 41.803 -27.208 -14.598 1.00 23.16 ?  9   TYR   B HD2  1 
ATOM   4061 H  HE1  . TYR   B 1 9   ? 45.399 -24.961 -16.418 1.00 24.42 ?  9   TYR   B HE1  1 
ATOM   4062 H  HE2  . TYR   B 1 9   ? 43.393 -26.274 -13.213 1.00 23.42 ?  9   TYR   B HE2  1 
ATOM   4063 H  HH   . TYR   B 1 9   ? 46.096 -24.592 -14.337 1.00 24.97 ?  9   TYR   B HH   1 
ATOM   4064 N  N    . LEU   B 1 10  ? 40.400 -30.193 -17.540 1.00 19.29 ?  10  LEU   B N    1 
ATOM   4065 C  CA   . LEU   B 1 10  ? 39.194 -30.955 -17.805 1.00 19.31 ?  10  LEU   B CA   1 
ATOM   4066 C  C    . LEU   B 1 10  ? 38.008 -30.187 -17.241 1.00 19.13 ?  10  LEU   B C    1 
ATOM   4067 O  O    . LEU   B 1 10  ? 38.027 -29.771 -16.078 1.00 18.89 ?  10  LEU   B O    1 
ATOM   4068 C  CB   . LEU   B 1 10  ? 39.300 -32.318 -17.125 1.00 20.20 ?  10  LEU   B CB   1 
ATOM   4069 C  CG   . LEU   B 1 10  ? 38.164 -33.286 -17.448 1.00 21.81 ?  10  LEU   B CG   1 
ATOM   4070 C  CD1  . LEU   B 1 10  ? 38.292 -33.792 -18.877 1.00 22.84 ?  10  LEU   B CD1  1 
ATOM   4071 C  CD2  . LEU   B 1 10  ? 38.135 -34.441 -16.460 1.00 22.95 ?  10  LEU   B CD2  1 
ATOM   4072 H  H    . LEU   B 1 10  ? 40.721 -30.342 -16.752 1.00 23.13 ?  10  LEU   B H    1 
ATOM   4073 H  HA   . LEU   B 1 10  ? 39.070 -31.083 -18.756 1.00 23.15 ?  10  LEU   B HA   1 
ATOM   4074 H  HB2  . LEU   B 1 10  ? 40.129 -32.741 -17.400 1.00 24.23 ?  10  LEU   B HB2  1 
ATOM   4075 H  HB3  . LEU   B 1 10  ? 39.306 -32.191 -16.161 1.00 24.23 ?  10  LEU   B HB3  1 
ATOM   4076 H  HG   . LEU   B 1 10  ? 37.318 -32.817 -17.374 1.00 26.15 ?  10  LEU   B HG   1 
ATOM   4077 H  HD11 . LEU   B 1 10  ? 37.606 -34.455 -19.039 1.00 27.40 ?  10  LEU   B HD11 1 
ATOM   4078 H  HD12 . LEU   B 1 10  ? 38.179 -33.043 -19.485 1.00 27.40 ?  10  LEU   B HD12 1 
ATOM   4079 H  HD13 . LEU   B 1 10  ? 39.170 -34.183 -18.994 1.00 27.40 ?  10  LEU   B HD13 1 
ATOM   4080 H  HD21 . LEU   B 1 10  ? 37.406 -35.036 -16.695 1.00 27.52 ?  10  LEU   B HD21 1 
ATOM   4081 H  HD22 . LEU   B 1 10  ? 38.979 -34.913 -16.505 1.00 27.52 ?  10  LEU   B HD22 1 
ATOM   4082 H  HD23 . LEU   B 1 10  ? 37.999 -34.086 -15.568 1.00 27.52 ?  10  LEU   B HD23 1 
ATOM   4083 N  N    . LYS   B 1 11  ? 36.982 -30.003 -18.065 1.00 20.15 ?  11  LYS   B N    1 
ATOM   4084 C  CA   . LYS   B 1 11  ? 35.783 -29.292 -17.649 1.00 22.34 ?  11  LYS   B CA   1 
ATOM   4085 C  C    . LYS   B 1 11  ? 34.919 -30.221 -16.800 1.00 21.33 ?  11  LYS   B C    1 
ATOM   4086 O  O    . LYS   B 1 11  ? 34.553 -31.317 -17.243 1.00 22.87 ?  11  LYS   B O    1 
ATOM   4087 C  CB   . LYS   B 1 11  ? 35.027 -28.837 -18.897 1.00 26.10 ?  11  LYS   B CB   1 
ATOM   4088 C  CG   . LYS   B 1 11  ? 33.882 -27.873 -18.654 1.00 29.53 ?  11  LYS   B CG   1 
ATOM   4089 C  CD   . LYS   B 1 11  ? 33.171 -27.556 -19.966 1.00 32.21 ?  11  LYS   B CD   1 
ATOM   4090 C  CE   . LYS   B 1 11  ? 32.132 -26.460 -19.798 1.00 34.21 ?  11  LYS   B CE   1 
ATOM   4091 N  NZ   . LYS   B 1 11  ? 32.758 -25.132 -19.558 1.00 35.29 ?  11  LYS   B NZ   1 
ATOM   4092 H  H    . LYS   B 1 11  ? 36.954 -30.284 -18.879 1.00 24.17 ?  11  LYS   B H    1 
ATOM   4093 H  HA   . LYS   B 1 11  ? 36.023 -28.512 -17.125 1.00 26.79 ?  11  LYS   B HA   1 
ATOM   4094 H  HB2  . LYS   B 1 11  ? 35.654 -28.394 -19.492 1.00 31.30 ?  11  LYS   B HB2  1 
ATOM   4095 H  HB3  . LYS   B 1 11  ? 34.660 -29.617 -19.339 1.00 31.30 ?  11  LYS   B HB3  1 
ATOM   4096 H  HG2  . LYS   B 1 11  ? 33.242 -28.277 -18.049 1.00 35.42 ?  11  LYS   B HG2  1 
ATOM   4097 H  HG3  . LYS   B 1 11  ? 34.227 -27.046 -18.285 1.00 35.42 ?  11  LYS   B HG3  1 
ATOM   4098 H  HD2  . LYS   B 1 11  ? 33.825 -27.257 -20.619 1.00 38.63 ?  11  LYS   B HD2  1 
ATOM   4099 H  HD3  . LYS   B 1 11  ? 32.722 -28.355 -20.286 1.00 38.63 ?  11  LYS   B HD3  1 
ATOM   4100 H  HE2  . LYS   B 1 11  ? 31.597 -26.403 -20.605 1.00 41.03 ?  11  LYS   B HE2  1 
ATOM   4101 H  HE3  . LYS   B 1 11  ? 31.569 -26.675 -19.038 1.00 41.03 ?  11  LYS   B HE3  1 
ATOM   4102 H  HZ1  . LYS   B 1 11  ? 32.128 -24.507 -19.489 1.00 42.33 ?  11  LYS   B HZ1  1 
ATOM   4103 H  HZ2  . LYS   B 1 11  ? 33.232 -25.150 -18.806 1.00 42.33 ?  11  LYS   B HZ2  1 
ATOM   4104 H  HZ3  . LYS   B 1 11  ? 33.297 -24.924 -20.236 1.00 42.33 ?  11  LYS   B HZ3  1 
ATOM   4105 N  N    . LEU   B 1 12  ? 34.598 -29.791 -15.578 1.00 19.47 ?  12  LEU   B N    1 
ATOM   4106 C  CA   . LEU   B 1 12  ? 33.641 -30.496 -14.731 1.00 18.65 ?  12  LEU   B CA   1 
ATOM   4107 C  C    . LEU   B 1 12  ? 32.253 -29.885 -14.822 1.00 18.32 ?  12  LEU   B C    1 
ATOM   4108 O  O    . LEU   B 1 12  ? 31.268 -30.603 -14.991 1.00 18.59 ?  12  LEU   B O    1 
ATOM   4109 C  CB   . LEU   B 1 12  ? 34.105 -30.514 -13.268 1.00 17.95 ?  12  LEU   B CB   1 
ATOM   4110 C  CG   . LEU   B 1 12  ? 35.448 -31.191 -12.997 1.00 17.57 ?  12  LEU   B CG   1 
ATOM   4111 C  CD1  . LEU   B 1 12  ? 35.803 -31.149 -11.521 1.00 17.66 ?  12  LEU   B CD1  1 
ATOM   4112 C  CD2  . LEU   B 1 12  ? 35.454 -32.627 -13.511 1.00 18.10 ?  12  LEU   B CD2  1 
ATOM   4113 H  H    . LEU   B 1 12  ? 34.921 -29.079 -15.215 1.00 23.35 ?  12  LEU   B H    1 
ATOM   4114 H  HA   . LEU   B 1 12  ? 33.567 -31.411 -15.036 1.00 22.37 ?  12  LEU   B HA   1 
ATOM   4115 H  HB2  . LEU   B 1 12  ? 34.168 -29.599 -12.958 1.00 21.52 ?  12  LEU   B HB2  1 
ATOM   4116 H  HB3  . LEU   B 1 12  ? 33.432 -30.983 -12.744 1.00 21.52 ?  12  LEU   B HB3  1 
ATOM   4117 H  HG   . LEU   B 1 12  ? 36.135 -30.704 -13.477 1.00 21.07 ?  12  LEU   B HG   1 
ATOM   4118 H  HD11 . LEU   B 1 12  ? 36.666 -31.582 -11.392 1.00 21.18 ?  12  LEU   B HD11 1 
ATOM   4119 H  HD12 . LEU   B 1 12  ? 35.857 -30.224 -11.232 1.00 21.18 ?  12  LEU   B HD12 1 
ATOM   4120 H  HD13 . LEU   B 1 12  ? 35.123 -31.616 -11.014 1.00 21.18 ?  12  LEU   B HD13 1 
ATOM   4121 H  HD21 . LEU   B 1 12  ? 36.261 -33.066 -13.204 1.00 21.70 ?  12  LEU   B HD21 1 
ATOM   4122 H  HD22 . LEU   B 1 12  ? 34.673 -33.087 -13.167 1.00 21.70 ?  12  LEU   B HD22 1 
ATOM   4123 H  HD23 . LEU   B 1 12  ? 35.430 -32.614 -14.481 1.00 21.70 ?  12  LEU   B HD23 1 
ATOM   4124 N  N    . THR   B 1 13  ? 32.164 -28.565 -14.710 1.00 18.20 ?  13  THR   B N    1 
ATOM   4125 C  CA   . THR   B 1 13  ? 30.937 -27.818 -14.922 1.00 18.38 ?  13  THR   B CA   1 
ATOM   4126 C  C    . THR   B 1 13  ? 31.277 -26.623 -15.807 1.00 20.35 ?  13  THR   B C    1 
ATOM   4127 O  O    . THR   B 1 13  ? 32.425 -26.438 -16.228 1.00 21.24 ?  13  THR   B O    1 
ATOM   4128 C  CB   . THR   B 1 13  ? 30.337 -27.337 -13.595 1.00 17.89 ?  13  THR   B CB   1 
ATOM   4129 O  OG1  . THR   B 1 13  ? 31.181 -26.318 -13.044 1.00 17.91 ?  13  THR   B OG1  1 
ATOM   4130 C  CG2  . THR   B 1 13  ? 30.207 -28.488 -12.601 1.00 18.41 ?  13  THR   B CG2  1 
ATOM   4131 H  H    . THR   B 1 13  ? 32.829 -28.058 -14.499 1.00 21.82 ?  13  THR   B H    1 
ATOM   4132 H  HA   . THR   B 1 13  ? 30.283 -28.378 -15.371 1.00 22.05 ?  13  THR   B HA   1 
ATOM   4133 H  HB   . THR   B 1 13  ? 29.446 -26.969 -13.757 1.00 21.45 ?  13  THR   B HB   1 
ATOM   4134 H  HG1  . THR   B 1 13  ? 30.878 -25.553 -13.248 1.00 21.47 ?  13  THR   B HG1  1 
ATOM   4135 H  HG21 . THR   B 1 13  ? 29.709 -28.199 -11.820 1.00 22.07 ?  13  THR   B HG21 1 
ATOM   4136 H  HG22 . THR   B 1 13  ? 29.737 -29.231 -13.014 1.00 22.07 ?  13  THR   B HG22 1 
ATOM   4137 H  HG23 . THR   B 1 13  ? 31.086 -28.786 -12.324 1.00 22.07 ?  13  THR   B HG23 1 
ATOM   4138 N  N    A ASP   B 1 14  ? 30.269 -25.796 -16.080 0.70 21.39 ?  14  ASP   B N    1 
ATOM   4139 N  N    B ASP   B 1 14  ? 30.271 -25.787 -16.076 0.30 21.05 ?  14  ASP   B N    1 
ATOM   4140 C  CA   A ASP   B 1 14  ? 30.489 -24.642 -16.942 0.70 22.71 ?  14  ASP   B CA   1 
ATOM   4141 C  CA   B ASP   B 1 14  ? 30.484 -24.635 -16.946 0.30 21.88 ?  14  ASP   B CA   1 
ATOM   4142 C  C    A ASP   B 1 14  ? 31.585 -23.730 -16.404 0.70 21.03 ?  14  ASP   B C    1 
ATOM   4143 C  C    B ASP   B 1 14  ? 31.501 -23.652 -16.385 0.30 20.37 ?  14  ASP   B C    1 
ATOM   4144 O  O    A ASP   B 1 14  ? 32.248 -23.040 -17.188 0.70 22.21 ?  14  ASP   B O    1 
ATOM   4145 O  O    B ASP   B 1 14  ? 32.003 -22.809 -17.137 0.30 20.75 ?  14  ASP   B O    1 
ATOM   4146 C  CB   A ASP   B 1 14  ? 29.188 -23.861 -17.123 0.70 26.07 ?  14  ASP   B CB   1 
ATOM   4147 C  CB   B ASP   B 1 14  ? 29.167 -23.899 -17.196 0.30 24.31 ?  14  ASP   B CB   1 
ATOM   4148 C  CG   A ASP   B 1 14  ? 28.208 -24.558 -18.043 0.70 29.61 ?  14  ASP   B CG   1 
ATOM   4149 C  CG   B ASP   B 1 14  ? 28.272 -24.628 -18.179 0.30 26.61 ?  14  ASP   B CG   1 
ATOM   4150 O  OD1  A ASP   B 1 14  ? 28.579 -25.572 -18.677 0.70 30.80 ?  14  ASP   B OD1  1 
ATOM   4151 O  OD1  B ASP   B 1 14  ? 28.807 -25.313 -19.077 0.30 27.44 ?  14  ASP   B OD1  1 
ATOM   4152 O  OD2  A ASP   B 1 14  ? 27.054 -24.090 -18.123 0.70 30.95 -1 14  ASP   B OD2  1 
ATOM   4153 O  OD2  B ASP   B 1 14  ? 27.034 -24.522 -18.054 0.30 27.37 -1 14  ASP   B OD2  1 
ATOM   4154 H  H    A ASP   B 1 14  ? 29.465 -25.871 -15.778 0.70 25.65 ?  14  ASP   B H    1 
ATOM   4155 H  H    B ASP   B 1 14  ? 29.469 -25.862 -15.773 0.30 25.24 ?  14  ASP   B H    1 
ATOM   4156 H  HA   A ASP   B 1 14  ? 30.776 -24.947 -17.813 0.70 27.23 ?  14  ASP   B HA   1 
ATOM   4157 H  HA   B ASP   B 1 14  ? 30.813 -24.947 -17.801 0.30 26.24 ?  14  ASP   B HA   1 
ATOM   4158 H  HB2  A ASP   B 1 14  ? 28.746 -23.768 -16.268 0.70 31.27 ?  14  ASP   B HB2  1 
ATOM   4159 H  HB2  B ASP   B 1 14  ? 28.688 -23.815 -16.357 0.30 29.16 ?  14  ASP   B HB2  1 
ATOM   4160 H  HB3  A ASP   B 1 14  ? 29.386 -22.987 -17.495 0.70 31.27 ?  14  ASP   B HB3  1 
ATOM   4161 H  HB3  B ASP   B 1 14  ? 29.366 -23.014 -17.551 0.30 29.16 ?  14  ASP   B HB3  1 
ATOM   4162 N  N    . ASN   B 1 15  ? 31.798 -23.715 -15.084 1.00 18.76 ?  15  ASN   B N    1 
ATOM   4163 C  CA   . ASN   B 1 15  ? 32.760 -22.799 -14.476 1.00 16.36 ?  15  ASN   B CA   1 
ATOM   4164 C  C    . ASN   B 1 15  ? 33.852 -23.456 -13.639 1.00 14.97 ?  15  ASN   B C    1 
ATOM   4165 O  O    . ASN   B 1 15  ? 34.707 -22.735 -13.110 1.00 15.06 ?  15  ASN   B O    1 
ATOM   4166 C  CB   . ASN   B 1 15  ? 32.046 -21.745 -13.615 1.00 16.62 ?  15  ASN   B CB   1 
ATOM   4167 C  CG   . ASN   B 1 15  ? 31.429 -22.341 -12.371 1.00 15.83 ?  15  ASN   B CG   1 
ATOM   4168 O  OD1  . ASN   B 1 15  ? 30.483 -23.135 -12.453 1.00 17.53 ?  15  ASN   B OD1  1 
ATOM   4169 N  ND2  . ASN   B 1 15  ? 31.961 -21.992 -11.215 1.00 14.92 ?  15  ASN   B ND2  1 
ATOM   4170 H  H    A ASN   B 1 15  ? 31.394 -24.226 -14.519 0.70 22.50 ?  15  ASN   B H    1 
ATOM   4171 H  H    B ASN   B 1 15  ? 31.431 -24.261 -14.526 0.30 22.50 ?  15  ASN   B H    1 
ATOM   4172 H  HA   . ASN   B 1 15  ? 33.206 -22.313 -15.181 1.00 19.61 ?  15  ASN   B HA   1 
ATOM   4173 H  HB2  . ASN   B 1 15  ? 32.689 -21.067 -13.341 1.00 19.93 ?  15  ASN   B HB2  1 
ATOM   4174 H  HB3  . ASN   B 1 15  ? 31.336 -21.328 -14.134 1.00 19.93 ?  15  ASN   B HB3  1 
ATOM   4175 H  HD21 . ASN   B 1 15  ? 31.644 -22.304 -10.477 1.00 17.88 ?  15  ASN   B HD21 1 
ATOM   4176 H  HD22 . ASN   B 1 15  ? 32.629 -21.443 -11.189 1.00 17.88 ?  15  ASN   B HD22 1 
ATOM   4177 N  N    . VAL   B 1 16  ? 33.860 -24.779 -13.493 1.00 14.93 ?  16  VAL   B N    1 
ATOM   4178 C  CA   . VAL   B 1 16  ? 34.858 -25.471 -12.681 1.00 14.66 ?  16  VAL   B CA   1 
ATOM   4179 C  C    . VAL   B 1 16  ? 35.653 -26.409 -13.574 1.00 15.12 ?  16  VAL   B C    1 
ATOM   4180 O  O    . VAL   B 1 16  ? 35.079 -27.294 -14.227 1.00 15.88 ?  16  VAL   B O    1 
ATOM   4181 C  CB   . VAL   B 1 16  ? 34.231 -26.236 -11.507 1.00 14.92 ?  16  VAL   B CB   1 
ATOM   4182 C  CG1  . VAL   B 1 16  ? 35.314 -26.969 -10.717 1.00 14.90 ?  16  VAL   B CG1  1 
ATOM   4183 C  CG2  . VAL   B 1 16  ? 33.431 -25.291 -10.614 1.00 15.60 ?  16  VAL   B CG2  1 
ATOM   4184 H  H    . VAL   B 1 16  ? 33.278 -25.306 -13.857 1.00 17.90 ?  16  VAL   B H    1 
ATOM   4185 H  HA   . VAL   B 1 16  ? 35.467 -24.812 -12.314 1.00 17.57 ?  16  VAL   B HA   1 
ATOM   4186 H  HB   . VAL   B 1 16  ? 33.617 -26.901 -11.860 1.00 17.89 ?  16  VAL   B HB   1 
ATOM   4187 H  HG11 . VAL   B 1 16  ? 34.938 -27.265 -9.873  1.00 17.87 ?  16  VAL   B HG11 1 
ATOM   4188 H  HG12 . VAL   B 1 16  ? 35.616 -27.735 -11.229 1.00 17.87 ?  16  VAL   B HG12 1 
ATOM   4189 H  HG13 . VAL   B 1 16  ? 36.051 -26.361 -10.557 1.00 17.87 ?  16  VAL   B HG13 1 
ATOM   4190 H  HG21 . VAL   B 1 16  ? 33.087 -25.790 -9.856  1.00 18.70 ?  16  VAL   B HG21 1 
ATOM   4191 H  HG22 . VAL   B 1 16  ? 34.010 -24.579 -10.308 1.00 18.70 ?  16  VAL   B HG22 1 
ATOM   4192 H  HG23 . VAL   B 1 16  ? 32.693 -24.922 -11.126 1.00 18.70 ?  16  VAL   B HG23 1 
ATOM   4193 N  N    . TYR   B 1 17  ? 36.976 -26.237 -13.558 1.00 15.15 ?  17  TYR   B N    1 
ATOM   4194 C  CA   . TYR   B 1 17  ? 37.920 -26.988 -14.370 1.00 15.62 ?  17  TYR   B CA   1 
ATOM   4195 C  C    . TYR   B 1 17  ? 38.971 -27.596 -13.453 1.00 14.46 ?  17  TYR   B C    1 
ATOM   4196 O  O    . TYR   B 1 17  ? 39.251 -27.063 -12.375 1.00 14.83 ?  17  TYR   B O    1 
ATOM   4197 C  CB   . TYR   B 1 17  ? 38.624 -26.062 -15.372 1.00 18.21 ?  17  TYR   B CB   1 
ATOM   4198 C  CG   . TYR   B 1 17  ? 37.695 -25.297 -16.285 1.00 21.33 ?  17  TYR   B CG   1 
ATOM   4199 C  CD1  . TYR   B 1 17  ? 37.116 -24.101 -15.881 1.00 22.99 ?  17  TYR   B CD1  1 
ATOM   4200 C  CD2  . TYR   B 1 17  ? 37.403 -25.769 -17.556 1.00 23.30 ?  17  TYR   B CD2  1 
ATOM   4201 C  CE1  . TYR   B 1 17  ? 36.265 -23.399 -16.718 1.00 24.54 ?  17  TYR   B CE1  1 
ATOM   4202 C  CE2  . TYR   B 1 17  ? 36.557 -25.076 -18.400 1.00 24.74 ?  17  TYR   B CE2  1 
ATOM   4203 C  CZ   . TYR   B 1 17  ? 35.991 -23.893 -17.975 1.00 25.61 ?  17  TYR   B CZ   1 
ATOM   4204 O  OH   . TYR   B 1 17  ? 35.148 -23.199 -18.812 1.00 26.85 ?  17  TYR   B OH   1 
ATOM   4205 H  H    . TYR   B 1 17  ? 37.367 -25.651 -13.059 1.00 18.16 ?  17  TYR   B H    1 
ATOM   4206 H  HA   . TYR   B 1 17  ? 37.454 -27.694 -14.854 1.00 18.72 ?  17  TYR   B HA   1 
ATOM   4207 H  HB2  . TYR   B 1 17  ? 39.158 -25.420 -14.883 1.00 21.84 ?  17  TYR   B HB2  1 
ATOM   4208 H  HB3  . TYR   B 1 17  ? 39.190 -26.603 -15.936 1.00 21.84 ?  17  TYR   B HB3  1 
ATOM   4209 H  HD1  . TYR   B 1 17  ? 37.299 -23.766 -15.034 1.00 27.58 ?  17  TYR   B HD1  1 
ATOM   4210 H  HD2  . TYR   B 1 17  ? 37.778 -26.568 -17.846 1.00 27.95 ?  17  TYR   B HD2  1 
ATOM   4211 H  HE1  . TYR   B 1 17  ? 35.882 -22.597 -16.437 1.00 29.43 ?  17  TYR   B HE1  1 
ATOM   4212 H  HE2  . TYR   B 1 17  ? 36.365 -25.406 -19.251 1.00 29.67 ?  17  TYR   B HE2  1 
ATOM   4213 H  HH   . TYR   B 1 17  ? 35.064 -23.603 -19.544 1.00 32.21 ?  17  TYR   B HH   1 
ATOM   4214 N  N    . ILE   B 1 18  ? 39.574 -28.706 -13.880 1.00 14.75 ?  18  ILE   B N    1 
ATOM   4215 C  CA   . ILE   B 1 18  ? 40.503 -29.431 -13.021 1.00 14.67 ?  18  ILE   B CA   1 
ATOM   4216 C  C    . ILE   B 1 18  ? 41.665 -29.979 -13.842 1.00 14.99 ?  18  ILE   B C    1 
ATOM   4217 O  O    . ILE   B 1 18  ? 41.506 -30.365 -15.006 1.00 16.20 ?  18  ILE   B O    1 
ATOM   4218 C  CB   . ILE   B 1 18  ? 39.757 -30.534 -12.222 1.00 15.11 ?  18  ILE   B CB   1 
ATOM   4219 C  CG1  . ILE   B 1 18  ? 40.629 -31.074 -11.084 1.00 15.53 ?  18  ILE   B CG1  1 
ATOM   4220 C  CG2  . ILE   B 1 18  ? 39.256 -31.655 -13.146 1.00 15.57 ?  18  ILE   B CG2  1 
ATOM   4221 C  CD1  . ILE   B 1 18  ? 39.841 -31.898 -10.066 1.00 16.90 ?  18  ILE   B CD1  1 
ATOM   4222 H  H    . ILE   B 1 18  ? 39.455 -29.059 -14.652 1.00 17.68 ?  18  ILE   B H    1 
ATOM   4223 H  HA   . ILE   B 1 18  ? 40.862 -28.815 -12.367 1.00 17.59 ?  18  ILE   B HA   1 
ATOM   4224 H  HB   . ILE   B 1 18  ? 38.973 -30.136 -11.811 1.00 18.12 ?  18  ILE   B HB   1 
ATOM   4225 H  HG12 . ILE   B 1 18  ? 41.318 -31.643 -11.453 1.00 18.62 ?  18  ILE   B HG12 1 
ATOM   4226 H  HG13 . ILE   B 1 18  ? 41.026 -30.327 -10.612 1.00 18.62 ?  18  ILE   B HG13 1 
ATOM   4227 H  HG21 . ILE   B 1 18  ? 38.674 -32.249 -12.641 1.00 18.67 ?  18  ILE   B HG21 1 
ATOM   4228 H  HG22 . ILE   B 1 18  ? 38.759 -31.255 -13.877 1.00 18.67 ?  18  ILE   B HG22 1 
ATOM   4229 H  HG23 . ILE   B 1 18  ? 40.014 -32.148 -13.489 1.00 18.67 ?  18  ILE   B HG23 1 
ATOM   4230 H  HD11 . ILE   B 1 18  ? 40.438 -32.174 -9.351  1.00 20.27 ?  18  ILE   B HD11 1 
ATOM   4231 H  HD12 . ILE   B 1 18  ? 39.123 -31.356 -9.703  1.00 20.27 ?  18  ILE   B HD12 1 
ATOM   4232 H  HD13 . ILE   B 1 18  ? 39.472 -32.681 -10.507 1.00 20.27 ?  18  ILE   B HD13 1 
ATOM   4233 N  N    . LYS   B 1 19  ? 42.840 -30.029 -13.212 1.00 15.49 ?  19  LYS   B N    1 
ATOM   4234 C  CA   . LYS   B 1 19  ? 44.055 -30.492 -13.866 1.00 16.38 ?  19  LYS   B CA   1 
ATOM   4235 C  C    . LYS   B 1 19  ? 44.960 -31.167 -12.846 1.00 16.18 ?  19  LYS   B C    1 
ATOM   4236 O  O    . LYS   B 1 19  ? 45.048 -30.735 -11.695 1.00 15.54 ?  19  LYS   B O    1 
ATOM   4237 C  CB   . LYS   B 1 19  ? 44.813 -29.320 -14.501 1.00 17.93 ?  19  LYS   B CB   1 
ATOM   4238 C  CG   . LYS   B 1 19  ? 45.988 -29.726 -15.367 1.00 19.94 ?  19  LYS   B CG   1 
ATOM   4239 C  CD   . LYS   B 1 19  ? 46.723 -28.499 -15.890 1.00 21.65 ?  19  LYS   B CD   1 
ATOM   4240 C  CE   . LYS   B 1 19  ? 47.875 -28.878 -16.800 1.00 23.35 ?  19  LYS   B CE   1 
ATOM   4241 N  NZ   . LYS   B 1 19  ? 48.650 -27.691 -17.248 1.00 24.01 ?  19  LYS   B NZ   1 
ATOM   4242 H  H    . LYS   B 1 19  ? 42.947 -29.792 -12.389 1.00 18.57 ?  19  LYS   B H    1 
ATOM   4243 H  HA   . LYS   B 1 19  ? 43.820 -31.130 -14.558 1.00 19.64 ?  19  LYS   B HA   1 
ATOM   4244 H  HB2  . LYS   B 1 19  ? 44.195 -28.823 -15.057 1.00 21.50 ?  19  LYS   B HB2  1 
ATOM   4245 H  HB3  . LYS   B 1 19  ? 45.145 -28.748 -13.789 1.00 21.50 ?  19  LYS   B HB3  1 
ATOM   4246 H  HG2  . LYS   B 1 19  ? 46.602 -30.260 -14.842 1.00 23.91 ?  19  LYS   B HG2  1 
ATOM   4247 H  HG3  . LYS   B 1 19  ? 45.658 -30.238 -16.125 1.00 23.91 ?  19  LYS   B HG3  1 
ATOM   4248 H  HD2  . LYS   B 1 19  ? 46.103 -27.946 -16.392 1.00 25.97 ?  19  LYS   B HD2  1 
ATOM   4249 H  HD3  . LYS   B 1 19  ? 47.080 -28.000 -15.137 1.00 25.97 ?  19  LYS   B HD3  1 
ATOM   4250 H  HE2  . LYS   B 1 19  ? 48.474 -29.473 -16.321 1.00 28.00 ?  19  LYS   B HE2  1 
ATOM   4251 H  HE3  . LYS   B 1 19  ? 47.521 -29.327 -17.586 1.00 28.00 ?  19  LYS   B HE3  1 
ATOM   4252 H  HZ1  . LYS   B 1 19  ? 49.287 -27.941 -17.816 1.00 28.80 ?  19  LYS   B HZ1  1 
ATOM   4253 H  HZ2  . LYS   B 1 19  ? 48.111 -27.111 -17.655 1.00 28.80 ?  19  LYS   B HZ2  1 
ATOM   4254 H  HZ3  . LYS   B 1 19  ? 49.027 -27.293 -16.548 1.00 28.80 ?  19  LYS   B HZ3  1 
ATOM   4255 N  N    . ASN   B 1 20  ? 45.644 -32.222 -13.281 1.00 17.38 ?  20  ASN   B N    1 
ATOM   4256 C  CA   . ASN   B 1 20  ? 46.670 -32.859 -12.461 1.00 18.51 ?  20  ASN   B CA   1 
ATOM   4257 C  C    . ASN   B 1 20  ? 47.945 -32.043 -12.646 1.00 18.74 ?  20  ASN   B C    1 
ATOM   4258 O  O    . ASN   B 1 20  ? 48.605 -32.134 -13.686 1.00 20.78 ?  20  ASN   B O    1 
ATOM   4259 C  CB   . ASN   B 1 20  ? 46.837 -34.315 -12.894 1.00 20.32 ?  20  ASN   B CB   1 
ATOM   4260 C  CG   . ASN   B 1 20  ? 47.998 -35.023 -12.211 1.00 21.82 ?  20  ASN   B CG   1 
ATOM   4261 O  OD1  . ASN   B 1 20  ? 48.658 -35.872 -12.822 1.00 24.07 ?  20  ASN   B OD1  1 
ATOM   4262 N  ND2  . ASN   B 1 20  ? 48.245 -34.702 -10.948 1.00 21.53 ?  20  ASN   B ND2  1 
ATOM   4263 H  H    . ASN   B 1 20  ? 45.535 -32.585 -14.052 1.00 20.84 ?  20  ASN   B H    1 
ATOM   4264 H  HA   . ASN   B 1 20  ? 46.398 -32.837 -11.528 1.00 22.20 ?  20  ASN   B HA   1 
ATOM   4265 H  HB2  . ASN   B 1 20  ? 46.021 -34.802 -12.678 1.00 24.36 ?  20  ASN   B HB2  1 
ATOM   4266 H  HB3  . ASN   B 1 20  ? 46.989 -34.341 -13.849 1.00 24.36 ?  20  ASN   B HB3  1 
ATOM   4267 H  HD21 . ASN   B 1 20  ? 48.894 -35.077 -10.527 1.00 25.82 ?  20  ASN   B HD21 1 
ATOM   4268 H  HD22 . ASN   B 1 20  ? 47.765 -34.109 -10.546 1.00 25.82 ?  20  ASN   B HD22 1 
ATOM   4269 N  N    . ALA   B 1 21  ? 48.288 -31.222 -11.649 1.00 18.18 ?  21  ALA   B N    1 
ATOM   4270 C  CA   . ALA   B 1 21  ? 49.414 -30.314 -11.803 1.00 18.86 ?  21  ALA   B CA   1 
ATOM   4271 C  C    . ALA   B 1 21  ? 49.879 -29.812 -10.444 1.00 17.81 ?  21  ALA   B C    1 
ATOM   4272 O  O    . ALA   B 1 21  ? 49.141 -29.842 -9.455  1.00 17.67 ?  21  ALA   B O    1 
ATOM   4273 C  CB   . ALA   B 1 21  ? 49.048 -29.133 -12.701 1.00 20.40 ?  21  ALA   B CB   1 
ATOM   4274 H  H    . ALA   B 1 21  ? 47.884 -31.177 -10.884 1.00 21.80 ?  21  ALA   B H    1 
ATOM   4275 H  HA   . ALA   B 1 21  ? 50.148 -30.798 -12.211 1.00 22.61 ?  21  ALA   B HA   1 
ATOM   4276 H  HB1  . ALA   B 1 21  ? 49.842 -28.597 -12.834 1.00 24.46 ?  21  ALA   B HB1  1 
ATOM   4277 H  HB2  . ALA   B 1 21  ? 48.730 -29.478 -13.547 1.00 24.46 ?  21  ALA   B HB2  1 
ATOM   4278 H  HB3  . ALA   B 1 21  ? 48.355 -28.614 -12.269 1.00 24.46 ?  21  ALA   B HB3  1 
ATOM   4279 N  N    . ASP   B 1 22  ? 51.133 -29.357 -10.432 1.00 17.17 ?  22  ASP   B N    1 
ATOM   4280 C  CA   . ASP   B 1 22  ? 51.753 -28.665 -9.306  1.00 16.35 ?  22  ASP   B CA   1 
ATOM   4281 C  C    . ASP   B 1 22  ? 51.346 -27.196 -9.383  1.00 14.92 ?  22  ASP   B C    1 
ATOM   4282 O  O    . ASP   B 1 22  ? 51.654 -26.521 -10.370 1.00 15.20 ?  22  ASP   B O    1 
ATOM   4283 C  CB   . ASP   B 1 22  ? 53.270 -28.840 -9.467  1.00 17.73 ?  22  ASP   B CB   1 
ATOM   4284 C  CG   . ASP   B 1 22  ? 54.099 -28.093 -8.430  1.00 19.32 ?  22  ASP   B CG   1 
ATOM   4285 O  OD1  . ASP   B 1 22  ? 53.741 -26.976 -8.021  1.00 19.31 ?  22  ASP   B OD1  1 
ATOM   4286 O  OD2  . ASP   B 1 22  ? 55.168 -28.617 -8.054  1.00 21.78 -1 22  ASP   B OD2  1 
ATOM   4287 H  H    . ASP   B 1 22  ? 51.670 -29.442 -11.102 1.00 20.59 ?  22  ASP   B H    1 
ATOM   4288 H  HA   . ASP   B 1 22  ? 51.466 -29.050 -8.461  1.00 19.61 ?  22  ASP   B HA   1 
ATOM   4289 H  HB2  . ASP   B 1 22  ? 53.493 -29.777 -9.396  1.00 21.26 ?  22  ASP   B HB2  1 
ATOM   4290 H  HB3  . ASP   B 1 22  ? 53.533 -28.500 -10.336 1.00 21.26 ?  22  ASP   B HB3  1 
ATOM   4291 N  N    . ILE   B 1 23  ? 50.637 -26.706 -8.359  1.00 13.90 ?  23  ILE   B N    1 
ATOM   4292 C  CA   . ILE   B 1 23  ? 50.046 -25.365 -8.425  1.00 13.49 ?  23  ILE   B CA   1 
ATOM   4293 C  C    . ILE   B 1 23  ? 51.102 -24.276 -8.570  1.00 13.09 ?  23  ILE   B C    1 
ATOM   4294 O  O    . ILE   B 1 23  ? 50.836 -23.234 -9.177  1.00 12.72 ?  23  ILE   B O    1 
ATOM   4295 C  CB   . ILE   B 1 23  ? 49.111 -25.117 -7.226  1.00 13.90 ?  23  ILE   B CB   1 
ATOM   4296 C  CG1  . ILE   B 1 23  ? 48.281 -23.849 -7.435  1.00 14.57 ?  23  ILE   B CG1  1 
ATOM   4297 C  CG2  . ILE   B 1 23  ? 49.884 -25.074 -5.924  1.00 14.97 ?  23  ILE   B CG2  1 
ATOM   4298 C  CD1  . ILE   B 1 23  ? 47.163 -23.674 -6.412  1.00 15.22 ?  23  ILE   B CD1  1 
ATOM   4299 H  H    . ILE   B 1 23  ? 50.486 -27.128 -7.628  1.00 16.66 ?  23  ILE   B H    1 
ATOM   4300 H  HA   . ILE   B 1 23  ? 49.497 -25.324 -9.222  1.00 16.17 ?  23  ILE   B HA   1 
ATOM   4301 H  HB   . ILE   B 1 23  ? 48.494 -25.864 -7.179  1.00 16.66 ?  23  ILE   B HB   1 
ATOM   4302 H  HG12 . ILE   B 1 23  ? 48.868 -23.076 -7.370  1.00 17.47 ?  23  ILE   B HG12 1 
ATOM   4303 H  HG13 . ILE   B 1 23  ? 47.878 -23.878 -8.319  1.00 17.47 ?  23  ILE   B HG13 1 
ATOM   4304 H  HG21 . ILE   B 1 23  ? 49.257 -25.072 -5.186  1.00 17.95 ?  23  ILE   B HG21 1 
ATOM   4305 H  HG22 . ILE   B 1 23  ? 50.455 -25.856 -5.872  1.00 17.95 ?  23  ILE   B HG22 1 
ATOM   4306 H  HG23 . ILE   B 1 23  ? 50.424 -24.269 -5.905  1.00 17.95 ?  23  ILE   B HG23 1 
ATOM   4307 H  HD11 . ILE   B 1 23  ? 46.638 -22.896 -6.651  1.00 18.24 ?  23  ILE   B HD11 1 
ATOM   4308 H  HD12 . ILE   B 1 23  ? 46.604 -24.468 -6.425  1.00 18.24 ?  23  ILE   B HD12 1 
ATOM   4309 H  HD13 . ILE   B 1 23  ? 47.555 -23.558 -5.535  1.00 18.24 ?  23  ILE   B HD13 1 
ATOM   4310 N  N    . VAL   B 1 24  ? 52.299 -24.479 -8.013  1.00 13.42 ?  24  VAL   B N    1 
ATOM   4311 C  CA   . VAL   B 1 24  ? 53.373 -23.498 -8.179  1.00 14.09 ?  24  VAL   B CA   1 
ATOM   4312 C  C    . VAL   B 1 24  ? 53.829 -23.455 -9.631  1.00 14.03 ?  24  VAL   B C    1 
ATOM   4313 O  O    . VAL   B 1 24  ? 53.978 -22.380 -10.226 1.00 14.67 ?  24  VAL   B O    1 
ATOM   4314 C  CB   . VAL   B 1 24  ? 54.547 -23.809 -7.228  1.00 15.09 ?  24  VAL   B CB   1 
ATOM   4315 C  CG1  . VAL   B 1 24  ? 55.756 -22.922 -7.547  1.00 15.76 ?  24  VAL   B CG1  1 
ATOM   4316 C  CG2  . VAL   B 1 24  ? 54.123 -23.624 -5.788  1.00 16.08 ?  24  VAL   B CG2  1 
ATOM   4317 H  H    . VAL   B 1 24  ? 52.513 -25.167 -7.540  1.00 16.09 ?  24  VAL   B H    1 
ATOM   4318 H  HA   . VAL   B 1 24  ? 53.035 -22.622 -7.947  1.00 16.89 ?  24  VAL   B HA   1 
ATOM   4319 H  HB   . VAL   B 1 24  ? 54.818 -24.736 -7.340  1.00 18.09 ?  24  VAL   B HB   1 
ATOM   4320 H  HG11 . VAL   B 1 24  ? 56.352 -22.916 -6.782  1.00 18.90 ?  24  VAL   B HG11 1 
ATOM   4321 H  HG12 . VAL   B 1 24  ? 56.214 -23.280 -8.321  1.00 18.90 ?  24  VAL   B HG12 1 
ATOM   4322 H  HG13 . VAL   B 1 24  ? 55.443 -22.022 -7.728  1.00 18.90 ?  24  VAL   B HG13 1 
ATOM   4323 H  HG21 . VAL   B 1 24  ? 54.843 -23.904 -5.204  1.00 19.28 ?  24  VAL   B HG21 1 
ATOM   4324 H  HG22 . VAL   B 1 24  ? 53.922 -22.686 -5.639  1.00 19.28 ?  24  VAL   B HG22 1 
ATOM   4325 H  HG23 . VAL   B 1 24  ? 53.332 -24.161 -5.619  1.00 19.28 ?  24  VAL   B HG23 1 
ATOM   4326 N  N    . GLU   B 1 25  ? 54.089 -24.628 -10.216 1.00 15.02 ?  25  GLU   B N    1 
ATOM   4327 C  CA   . GLU   B 1 25  ? 54.482 -24.665 -11.619 1.00 16.64 ?  25  GLU   B CA   1 
ATOM   4328 C  C    . GLU   B 1 25  ? 53.372 -24.124 -12.508 1.00 15.36 ?  25  GLU   B C    1 
ATOM   4329 O  O    . GLU   B 1 25  ? 53.638 -23.401 -13.476 1.00 16.30 ?  25  GLU   B O    1 
ATOM   4330 C  CB   . GLU   B 1 25  ? 54.880 -26.086 -12.017 1.00 20.68 ?  25  GLU   B CB   1 
ATOM   4331 C  CG   . GLU   B 1 25  ? 56.182 -26.536 -11.367 1.00 26.35 ?  25  GLU   B CG   1 
ATOM   4332 C  CD   . GLU   B 1 25  ? 57.299 -25.505 -11.475 1.00 31.12 ?  25  GLU   B CD   1 
ATOM   4333 O  OE1  . GLU   B 1 25  ? 57.688 -25.161 -12.612 1.00 33.26 ?  25  GLU   B OE1  1 
ATOM   4334 O  OE2  . GLU   B 1 25  ? 57.781 -25.024 -10.422 1.00 33.05 -1 25  GLU   B OE2  1 
ATOM   4335 H  H    . GLU   B 1 25  ? 54.048 -25.396 -9.828  1.00 18.01 ?  25  GLU   B H    1 
ATOM   4336 H  HA   . GLU   B 1 25  ? 55.242 -24.080 -11.743 1.00 19.95 ?  25  GLU   B HA   1 
ATOM   4337 H  HB2  . GLU   B 1 25  ? 54.179 -26.700 -11.739 1.00 24.80 ?  25  GLU   B HB2  1 
ATOM   4338 H  HB3  . GLU   B 1 25  ? 54.990 -26.125 -12.980 1.00 24.80 ?  25  GLU   B HB3  1 
ATOM   4339 H  HG2  . GLU   B 1 25  ? 56.027 -26.695 -10.428 1.00 31.61 ?  25  GLU   B HG2  1 
ATOM   4340 H  HG3  . GLU   B 1 25  ? 56.487 -27.344 -11.805 1.00 31.61 ?  25  GLU   B HG3  1 
ATOM   4341 N  N    . GLU   B 1 26  ? 52.120 -24.446 -12.180 1.00 14.51 ?  26  GLU   B N    1 
ATOM   4342 C  CA   . GLU   B 1 26  ? 50.997 -23.916 -12.943 1.00 15.03 ?  26  GLU   B CA   1 
ATOM   4343 C  C    . GLU   B 1 26  ? 50.949 -22.398 -12.864 1.00 14.41 ?  26  GLU   B C    1 
ATOM   4344 O  O    . GLU   B 1 26  ? 50.752 -21.722 -13.877 1.00 15.72 ?  26  GLU   B O    1 
ATOM   4345 C  CB   . GLU   B 1 26  ? 49.684 -24.499 -12.422 1.00 17.02 ?  26  GLU   B CB   1 
ATOM   4346 C  CG   . GLU   B 1 26  ? 49.250 -25.783 -13.100 1.00 20.72 ?  26  GLU   B CG   1 
ATOM   4347 C  CD   . GLU   B 1 26  ? 49.003 -25.625 -14.600 1.00 22.11 ?  26  GLU   B CD   1 
ATOM   4348 O  OE1  . GLU   B 1 26  ? 48.026 -24.962 -15.016 1.00 22.31 ?  26  GLU   B OE1  1 
ATOM   4349 O  OE2  . GLU   B 1 26  ? 49.792 -26.192 -15.367 1.00 24.39 -1 26  GLU   B OE2  1 
ATOM   4350 H  H    . GLU   B 1 26  ? 51.894 -24.966 -11.528 1.00 17.39 ?  26  GLU   B H    1 
ATOM   4351 H  HA   . GLU   B 1 26  ? 51.095 -24.168 -13.872 1.00 18.02 ?  26  GLU   B HA   1 
ATOM   4352 H  HB2  . GLU   B 1 26  ? 49.777 -24.684 -11.472 1.00 20.41 ?  26  GLU   B HB2  1 
ATOM   4353 H  HB3  . GLU   B 1 26  ? 48.977 -23.844 -12.553 1.00 20.41 ?  26  GLU   B HB3  1 
ATOM   4354 H  HG2  . GLU   B 1 26  ? 49.955 -26.433 -12.991 1.00 24.85 ?  26  GLU   B HG2  1 
ATOM   4355 H  HG3  . GLU   B 1 26  ? 48.433 -26.095 -12.681 1.00 24.85 ?  26  GLU   B HG3  1 
ATOM   4356 N  N    . ALA   B 1 27  ? 51.096 -21.846 -11.659 1.00 13.40 ?  27  ALA   B N    1 
ATOM   4357 C  CA   . ALA   B 1 27  ? 51.059 -20.397 -11.512 1.00 13.76 ?  27  ALA   B CA   1 
ATOM   4358 C  C    . ALA   B 1 27  ? 52.128 -19.734 -12.374 1.00 14.76 ?  27  ALA   B C    1 
ATOM   4359 O  O    . ALA   B 1 27  ? 51.866 -18.729 -13.053 1.00 15.50 ?  27  ALA   B O    1 
ATOM   4360 C  CB   . ALA   B 1 27  ? 51.215 -20.013 -10.039 1.00 13.76 ?  27  ALA   B CB   1 
ATOM   4361 H  H    . ALA   B 1 27  ? 51.207 -22.283 -10.922 1.00 16.07 ?  27  ALA   B H    1 
ATOM   4362 H  HA   . ALA   B 1 27  ? 50.198 -20.071 -11.807 1.00 16.49 ?  27  ALA   B HA   1 
ATOM   4363 H  HB1  . ALA   B 1 27  ? 51.183 -19.046 -9.958  1.00 16.50 ?  27  ALA   B HB1  1 
ATOM   4364 H  HB2  . ALA   B 1 27  ? 50.484 -20.407 -9.531  1.00 16.50 ?  27  ALA   B HB2  1 
ATOM   4365 H  HB3  . ALA   B 1 27  ? 52.062 -20.346 -9.709  1.00 16.50 ?  27  ALA   B HB3  1 
ATOM   4366 N  N    . LYS   B 1 28  ? 53.341 -20.287 -12.374 1.00 16.41 ?  28  LYS   B N    1 
ATOM   4367 C  CA   . LYS   B 1 28  ? 54.414 -19.672 -13.146 1.00 18.59 ?  28  LYS   B CA   1 
ATOM   4368 C  C    . LYS   B 1 28  ? 54.157 -19.758 -14.645 1.00 19.44 ?  28  LYS   B C    1 
ATOM   4369 O  O    . LYS   B 1 28  ? 54.568 -18.863 -15.395 1.00 20.45 ?  28  LYS   B O    1 
ATOM   4370 C  CB   . LYS   B 1 28  ? 55.767 -20.275 -12.757 1.00 22.14 ?  28  LYS   B CB   1 
ATOM   4371 C  CG   . LYS   B 1 28  ? 56.167 -19.924 -11.327 1.00 25.71 ?  28  LYS   B CG   1 
ATOM   4372 C  CD   . LYS   B 1 28  ? 57.595 -20.323 -10.983 1.00 30.60 ?  28  LYS   B CD   1 
ATOM   4373 C  CE   . LYS   B 1 28  ? 57.704 -21.796 -10.664 1.00 35.05 ?  28  LYS   B CE   1 
ATOM   4374 N  NZ   . LYS   B 1 28  ? 59.055 -22.138 -10.133 1.00 37.18 ?  28  LYS   B NZ   1 
ATOM   4375 H  H    . LYS   B 1 28  ? 53.566 -20.999 -11.941 1.00 19.67 ?  28  LYS   B H    1 
ATOM   4376 H  HA   . LYS   B 1 28  ? 54.449 -18.733 -12.923 1.00 22.30 ?  28  LYS   B HA   1 
ATOM   4377 H  HB2  . LYS   B 1 28  ? 55.721 -21.240 -12.827 1.00 26.55 ?  28  LYS   B HB2  1 
ATOM   4378 H  HB3  . LYS   B 1 28  ? 56.452 -19.930 -13.354 1.00 26.55 ?  28  LYS   B HB3  1 
ATOM   4379 H  HG2  . LYS   B 1 28  ? 56.089 -18.963 -11.210 1.00 30.84 ?  28  LYS   B HG2  1 
ATOM   4380 H  HG3  . LYS   B 1 28  ? 55.572 -20.380 -10.716 1.00 30.84 ?  28  LYS   B HG3  1 
ATOM   4381 H  HD2  . LYS   B 1 28  ? 58.171 -20.131 -11.739 1.00 36.71 ?  28  LYS   B HD2  1 
ATOM   4382 H  HD3  . LYS   B 1 28  ? 57.885 -19.820 -10.205 1.00 36.71 ?  28  LYS   B HD3  1 
ATOM   4383 H  HE2  . LYS   B 1 28  ? 57.044 -22.027 -9.992  1.00 42.04 ?  28  LYS   B HE2  1 
ATOM   4384 H  HE3  . LYS   B 1 28  ? 57.554 -22.311 -11.472 1.00 42.04 ?  28  LYS   B HE3  1 
ATOM   4385 H  HZ1  . LYS   B 1 28  ? 59.099 -23.008 -9.952  1.00 44.60 ?  28  LYS   B HZ1  1 
ATOM   4386 H  HZ2  . LYS   B 1 28  ? 59.678 -21.936 -10.735 1.00 44.60 ?  28  LYS   B HZ2  1 
ATOM   4387 H  HZ3  . LYS   B 1 28  ? 59.214 -21.679 -9.387  1.00 44.60 ?  28  LYS   B HZ3  1 
ATOM   4388 N  N    . LYS   B 1 29  ? 53.449 -20.795 -15.095 1.00 20.65 ?  29  LYS   B N    1 
ATOM   4389 C  CA   . LYS   B 1 29  ? 53.166 -20.951 -16.517 1.00 23.36 ?  29  LYS   B CA   1 
ATOM   4390 C  C    . LYS   B 1 29  ? 51.913 -20.200 -16.956 1.00 21.92 ?  29  LYS   B C    1 
ATOM   4391 O  O    . LYS   B 1 29  ? 51.903 -19.599 -18.036 1.00 23.02 ?  29  LYS   B O    1 
ATOM   4392 C  CB   . LYS   B 1 29  ? 53.041 -22.435 -16.868 1.00 28.25 ?  29  LYS   B CB   1 
ATOM   4393 C  CG   . LYS   B 1 29  ? 52.906 -22.711 -18.357 1.00 32.95 ?  29  LYS   B CG   1 
ATOM   4394 C  CD   . LYS   B 1 29  ? 53.122 -24.187 -18.671 1.00 36.67 ?  29  LYS   B CD   1 
ATOM   4395 C  CE   . LYS   B 1 29  ? 51.979 -25.053 -18.163 1.00 39.22 ?  29  LYS   B CE   1 
ATOM   4396 N  NZ   . LYS   B 1 29  ? 52.222 -26.501 -18.428 1.00 40.67 ?  29  LYS   B NZ   1 
ATOM   4397 H  H    . LYS   B 1 29  ? 53.115 -21.420 -14.593 1.00 24.76 ?  29  LYS   B H    1 
ATOM   4398 H  HA   . LYS   B 1 29  ? 53.908 -20.594 -17.015 1.00 28.01 ?  29  LYS   B HA   1 
ATOM   4399 H  HB2  . LYS   B 1 29  ? 53.838 -22.890 -16.556 1.00 33.88 ?  29  LYS   B HB2  1 
ATOM   4400 H  HB3  . LYS   B 1 29  ? 52.260 -22.797 -16.429 1.00 33.88 ?  29  LYS   B HB3  1 
ATOM   4401 H  HG2  . LYS   B 1 29  ? 52.014 -22.464 -18.648 1.00 39.53 ?  29  LYS   B HG2  1 
ATOM   4402 H  HG3  . LYS   B 1 29  ? 53.571 -22.195 -18.841 1.00 39.53 ?  29  LYS   B HG3  1 
ATOM   4403 H  HD2  . LYS   B 1 29  ? 53.185 -24.302 -19.631 1.00 43.99 ?  29  LYS   B HD2  1 
ATOM   4404 H  HD3  . LYS   B 1 29  ? 53.940 -24.487 -18.244 1.00 43.99 ?  29  LYS   B HD3  1 
ATOM   4405 H  HE2  . LYS   B 1 29  ? 51.885 -24.933 -17.205 1.00 47.04 ?  29  LYS   B HE2  1 
ATOM   4406 H  HE3  . LYS   B 1 29  ? 51.159 -24.796 -18.614 1.00 47.04 ?  29  LYS   B HE3  1 
ATOM   4407 H  HZ1  . LYS   B 1 29  ? 51.540 -26.986 -18.123 1.00 48.79 ?  29  LYS   B HZ1  1 
ATOM   4408 H  HZ2  . LYS   B 1 29  ? 52.306 -26.641 -19.303 1.00 48.79 ?  29  LYS   B HZ2  1 
ATOM   4409 H  HZ3  . LYS   B 1 29  ? 52.968 -26.764 -18.020 1.00 48.79 ?  29  LYS   B HZ3  1 
ATOM   4410 N  N    . VAL   B 1 30  ? 50.858 -20.230 -16.136 1.00 19.97 ?  30  VAL   B N    1 
ATOM   4411 C  CA   . VAL   B 1 30  ? 49.567 -19.643 -16.502 1.00 20.21 ?  30  VAL   B CA   1 
ATOM   4412 C  C    . VAL   B 1 30  ? 49.576 -18.129 -16.368 1.00 19.12 ?  30  VAL   B C    1 
ATOM   4413 O  O    . VAL   B 1 30  ? 48.840 -17.428 -17.081 1.00 20.24 ?  30  VAL   B O    1 
ATOM   4414 C  CB   . VAL   B 1 30  ? 48.469 -20.250 -15.607 1.00 21.16 ?  30  VAL   B CB   1 
ATOM   4415 C  CG1  . VAL   B 1 30  ? 47.190 -19.426 -15.666 1.00 21.48 ?  30  VAL   B CG1  1 
ATOM   4416 C  CG2  . VAL   B 1 30  ? 48.203 -21.700 -15.990 1.00 21.98 ?  30  VAL   B CG2  1 
ATOM   4417 H  H    . VAL   B 1 30  ? 50.853 -20.605 -15.353 1.00 23.95 ?  30  VAL   B H    1 
ATOM   4418 H  HA   . VAL   B 1 30  ? 49.360 -19.878 -17.419 1.00 24.23 ?  30  VAL   B HA   1 
ATOM   4419 H  HB   . VAL   B 1 30  ? 48.775 -20.253 -14.687 1.00 25.37 ?  30  VAL   B HB   1 
ATOM   4420 H  HG11 . VAL   B 1 30  ? 46.445 -19.996 -15.418 1.00 25.76 ?  30  VAL   B HG11 1 
ATOM   4421 H  HG12 . VAL   B 1 30  ? 47.258 -18.689 -15.041 1.00 25.76 ?  30  VAL   B HG12 1 
ATOM   4422 H  HG13 . VAL   B 1 30  ? 47.060 -19.102 -16.566 1.00 25.76 ?  30  VAL   B HG13 1 
ATOM   4423 H  HG21 . VAL   B 1 30  ? 47.518 -22.066 -15.403 1.00 26.36 ?  30  VAL   B HG21 1 
ATOM   4424 H  HG22 . VAL   B 1 30  ? 47.894 -21.734 -16.910 1.00 26.36 ?  30  VAL   B HG22 1 
ATOM   4425 H  HG23 . VAL   B 1 30  ? 49.021 -22.209 -15.896 1.00 26.36 ?  30  VAL   B HG23 1 
ATOM   4426 N  N    . LYS   B 1 31  ? 50.351 -17.615 -15.431 1.00 18.36 ?  31  LYS   B N    1 
ATOM   4427 C  CA   . LYS   B 1 31  ? 50.380 -16.203 -15.085 1.00 18.84 ?  31  LYS   B CA   1 
ATOM   4428 C  C    . LYS   B 1 31  ? 48.984 -15.718 -14.692 1.00 16.78 ?  31  LYS   B C    1 
ATOM   4429 O  O    . LYS   B 1 31  ? 48.446 -14.792 -15.314 1.00 17.51 ?  31  LYS   B O    1 
ATOM   4430 C  CB   . LYS   B 1 31  ? 51.015 -15.401 -16.227 1.00 21.88 ?  31  LYS   B CB   1 
ATOM   4431 C  CG   . LYS   B 1 31  ? 52.449 -15.842 -16.529 1.00 25.21 ?  31  LYS   B CG   1 
ATOM   4432 C  CD   . LYS   B 1 31  ? 53.036 -15.084 -17.702 1.00 28.96 ?  31  LYS   B CD   1 
ATOM   4433 C  CE   . LYS   B 1 31  ? 54.526 -15.316 -17.824 1.00 31.93 ?  31  LYS   B CE   1 
ATOM   4434 N  NZ   . LYS   B 1 31  ? 55.227 -14.889 -16.585 1.00 33.39 ?  31  LYS   B NZ   1 
ATOM   4435 H  H    . LYS   B 1 31  ? 50.893 -18.094 -14.970 1.00 22.01 ?  31  LYS   B H    1 
ATOM   4436 H  HA   . LYS   B 1 31  ? 50.941 -16.109 -14.316 1.00 22.60 ?  31  LYS   B HA   1 
ATOM   4437 H  HB2  . LYS   B 1 31  ? 50.494 -15.518 -17.037 1.00 26.24 ?  31  LYS   B HB2  1 
ATOM   4438 H  HB3  . LYS   B 1 31  ? 51.039 -14.468 -15.975 1.00 26.24 ?  31  LYS   B HB3  1 
ATOM   4439 H  HG2  . LYS   B 1 31  ? 52.998 -15.680 -15.746 1.00 30.23 ?  31  LYS   B HG2  1 
ATOM   4440 H  HG3  . LYS   B 1 31  ? 52.455 -16.790 -16.747 1.00 30.23 ?  31  LYS   B HG3  1 
ATOM   4441 H  HD2  . LYS   B 1 31  ? 52.612 -15.388 -18.517 1.00 34.73 ?  31  LYS   B HD2  1 
ATOM   4442 H  HD3  . LYS   B 1 31  ? 52.885 -14.138 -17.571 1.00 34.73 ?  31  LYS   B HD3  1 
ATOM   4443 H  HE2  . LYS   B 1 31  ? 54.699 -16.261 -17.965 1.00 38.29 ?  31  LYS   B HE2  1 
ATOM   4444 H  HE3  . LYS   B 1 31  ? 54.872 -14.796 -18.568 1.00 38.29 ?  31  LYS   B HE3  1 
ATOM   4445 H  HZ1  . LYS   B 1 31  ? 56.105 -14.869 -16.723 1.00 40.06 ?  31  LYS   B HZ1  1 
ATOM   4446 H  HZ2  . LYS   B 1 31  ? 54.953 -14.076 -16.348 1.00 40.06 ?  31  LYS   B HZ2  1 
ATOM   4447 H  HZ3  . LYS   B 1 31  ? 55.050 -15.458 -15.924 1.00 40.06 ?  31  LYS   B HZ3  1 
ATOM   4448 N  N    . PRO   B 1 32  ? 48.376 -16.309 -13.658 1.00 14.52 ?  32  PRO   B N    1 
ATOM   4449 C  CA   . PRO   B 1 32  ? 47.004 -15.943 -13.292 1.00 13.87 ?  32  PRO   B CA   1 
ATOM   4450 C  C    . PRO   B 1 32  ? 46.925 -14.599 -12.583 1.00 13.81 ?  32  PRO   B C    1 
ATOM   4451 O  O    . PRO   B 1 32  ? 47.847 -14.179 -11.879 1.00 15.20 ?  32  PRO   B O    1 
ATOM   4452 C  CB   . PRO   B 1 32  ? 46.605 -17.059 -12.320 1.00 14.01 ?  32  PRO   B CB   1 
ATOM   4453 C  CG   . PRO   B 1 32  ? 47.906 -17.406 -11.648 1.00 14.15 ?  32  PRO   B CG   1 
ATOM   4454 C  CD   . PRO   B 1 32  ? 48.952 -17.295 -12.720 1.00 14.49 ?  32  PRO   B CD   1 
ATOM   4455 H  HA   . PRO   B 1 32  ? 46.419 -15.955 -14.069 1.00 16.62 ?  32  PRO   B HA   1 
ATOM   4456 H  HB2  . PRO   B 1 32  ? 45.959 -16.725 -11.679 1.00 16.80 ?  32  PRO   B HB2  1 
ATOM   4457 H  HB3  . PRO   B 1 32  ? 46.254 -17.819 -12.809 1.00 16.80 ?  32  PRO   B HB3  1 
ATOM   4458 H  HG2  . PRO   B 1 32  ? 48.083 -16.775 -10.929 1.00 16.97 ?  32  PRO   B HG2  1 
ATOM   4459 H  HG3  . PRO   B 1 32  ? 47.868 -18.313 -11.303 1.00 16.97 ?  32  PRO   B HG3  1 
ATOM   4460 H  HD2  . PRO   B 1 32  ? 49.779 -16.958 -12.351 1.00 17.37 ?  32  PRO   B HD2  1 
ATOM   4461 H  HD3  . PRO   B 1 32  ? 49.070 -18.145 -13.162 1.00 17.37 ?  32  PRO   B HD3  1 
ATOM   4462 N  N    . THR   B 1 33  ? 45.778 -13.938 -12.753 1.00 13.42 ?  33  THR   B N    1 
ATOM   4463 C  CA   . THR   B 1 33  ? 45.488 -12.760 -11.944 1.00 13.66 ?  33  THR   B CA   1 
ATOM   4464 C  C    . THR   B 1 33  ? 45.443 -13.117 -10.462 1.00 13.45 ?  33  THR   B C    1 
ATOM   4465 O  O    . THR   B 1 33  ? 45.923 -12.344 -9.619  1.00 14.58 ?  33  THR   B O    1 
ATOM   4466 C  CB   . THR   B 1 33  ? 44.169 -12.122 -12.393 1.00 14.44 ?  33  THR   B CB   1 
ATOM   4467 O  OG1  . THR   B 1 33  ? 44.209 -11.870 -13.801 1.00 14.30 ?  33  THR   B OG1  1 
ATOM   4468 C  CG2  . THR   B 1 33  ? 43.921 -10.821 -11.643 1.00 15.71 ?  33  THR   B CG2  1 
ATOM   4469 H  H    . THR   B 1 33  ? 45.160 -14.151 -13.321 1.00 16.08 ?  33  THR   B H    1 
ATOM   4470 H  HA   . THR   B 1 33  ? 46.192 -12.111 -12.074 1.00 16.37 ?  33  THR   B HA   1 
ATOM   4471 H  HB   . THR   B 1 33  ? 43.435 -12.732 -12.202 1.00 17.31 ?  33  THR   B HB   1 
ATOM   4472 H  HG1  . THR   B 1 33  ? 43.492 -11.506 -14.050 1.00 17.15 ?  33  THR   B HG1  1 
ATOM   4473 H  HG21 . THR   B 1 33  ? 43.169 -10.355 -12.030 1.00 18.83 ?  33  THR   B HG21 1 
ATOM   4474 H  HG22 . THR   B 1 33  ? 43.734 -11.008 -10.709 1.00 18.83 ?  33  THR   B HG22 1 
ATOM   4475 H  HG23 . THR   B 1 33  ? 44.709 -10.256 -11.699 1.00 18.83 ?  33  THR   B HG23 1 
ATOM   4476 N  N    . VAL   B 1 34  ? 44.884 -14.285 -10.123 1.00 12.51 ?  34  VAL   B N    1 
ATOM   4477 C  CA   . VAL   B 1 34  ? 44.687 -14.683 -8.732  1.00 12.17 ?  34  VAL   B CA   1 
ATOM   4478 C  C    . VAL   B 1 34  ? 45.112 -16.133 -8.564  1.00 11.38 ?  34  VAL   B C    1 
ATOM   4479 O  O    . VAL   B 1 34  ? 44.589 -17.023 -9.245  1.00 12.05 ?  34  VAL   B O    1 
ATOM   4480 C  CB   . VAL   B 1 34  ? 43.217 -14.539 -8.281  1.00 13.27 ?  34  VAL   B CB   1 
ATOM   4481 C  CG1  . VAL   B 1 34  ? 43.060 -14.987 -6.838  1.00 13.55 ?  34  VAL   B CG1  1 
ATOM   4482 C  CG2  . VAL   B 1 34  ? 42.723 -13.109 -8.456  1.00 14.41 ?  34  VAL   B CG2  1 
ATOM   4483 H  H    . VAL   B 1 34  ? 44.613 -14.876 -10.691 1.00 15.00 ?  34  VAL   B H    1 
ATOM   4484 H  HA   . VAL   B 1 34  ? 45.241 -14.129 -8.156  1.00 14.59 ?  34  VAL   B HA   1 
ATOM   4485 H  HB   . VAL   B 1 34  ? 42.664 -15.110 -8.833  1.00 15.91 ?  34  VAL   B HB   1 
ATOM   4486 H  HG11 . VAL   B 1 34  ? 42.212 -14.665 -6.495  1.00 16.25 ?  34  VAL   B HG11 1 
ATOM   4487 H  HG12 . VAL   B 1 34  ? 43.079 -15.959 -6.801  1.00 16.25 ?  34  VAL   B HG12 1 
ATOM   4488 H  HG13 . VAL   B 1 34  ? 43.788 -14.624 -6.309  1.00 16.25 ?  34  VAL   B HG13 1 
ATOM   4489 H  HG21 . VAL   B 1 34  ? 41.804 -13.050 -8.149  1.00 17.27 ?  34  VAL   B HG21 1 
ATOM   4490 H  HG22 . VAL   B 1 34  ? 43.283 -12.512 -7.933  1.00 17.27 ?  34  VAL   B HG22 1 
ATOM   4491 H  HG23 . VAL   B 1 34  ? 42.772 -12.867 -9.395  1.00 17.27 ?  34  VAL   B HG23 1 
ATOM   4492 N  N    . VAL   B 1 35  ? 46.018 -16.381 -7.622  1.00 10.74 ?  35  VAL   B N    1 
ATOM   4493 C  CA   . VAL   B 1 35  ? 46.250 -17.724 -7.100  1.00 10.66 ?  35  VAL   B CA   1 
ATOM   4494 C  C    . VAL   B 1 35  ? 45.712 -17.777 -5.678  1.00 10.17 ?  35  VAL   B C    1 
ATOM   4495 O  O    . VAL   B 1 35  ? 45.934 -16.854 -4.889  1.00 10.71 ?  35  VAL   B O    1 
ATOM   4496 C  CB   . VAL   B 1 35  ? 47.728 -18.152 -7.185  1.00 11.46 ?  35  VAL   B CB   1 
ATOM   4497 C  CG1  . VAL   B 1 35  ? 48.632 -17.305 -6.276  1.00 12.01 ?  35  VAL   B CG1  1 
ATOM   4498 C  CG2  . VAL   B 1 35  ? 47.870 -19.644 -6.851  1.00 11.65 ?  35  VAL   B CG2  1 
ATOM   4499 H  H    . VAL   B 1 35  ? 46.519 -15.778 -7.261  1.00 12.87 ?  35  VAL   B H    1 
ATOM   4500 H  HA   . VAL   B 1 35  ? 45.729 -18.349 -7.623  1.00 12.78 ?  35  VAL   B HA   1 
ATOM   4501 H  HB   . VAL   B 1 35  ? 48.028 -18.032 -8.100  1.00 13.73 ?  35  VAL   B HB   1 
ATOM   4502 H  HG11 . VAL   B 1 35  ? 49.553 -17.536 -6.456  1.00 14.40 ?  35  VAL   B HG11 1 
ATOM   4503 H  HG12 . VAL   B 1 35  ? 48.471 -16.373 -6.463  1.00 14.40 ?  35  VAL   B HG12 1 
ATOM   4504 H  HG13 . VAL   B 1 35  ? 48.412 -17.505 -5.351  1.00 14.40 ?  35  VAL   B HG13 1 
ATOM   4505 H  HG21 . VAL   B 1 35  ? 48.790 -19.915 -6.965  1.00 13.97 ?  35  VAL   B HG21 1 
ATOM   4506 H  HG22 . VAL   B 1 35  ? 47.591 -19.796 -5.930  1.00 13.97 ?  35  VAL   B HG22 1 
ATOM   4507 H  HG23 . VAL   B 1 35  ? 47.298 -20.165 -7.448  1.00 13.97 ?  35  VAL   B HG23 1 
ATOM   4508 N  N    . VAL   B 1 36  ? 44.984 -18.851 -5.361  1.00 10.12 ?  36  VAL   B N    1 
ATOM   4509 C  CA   . VAL   B 1 36  ? 44.445 -19.052 -4.025  1.00 9.91  ?  36  VAL   B CA   1 
ATOM   4510 C  C    . VAL   B 1 36  ? 45.455 -19.812 -3.175  1.00 9.61  ?  36  VAL   B C    1 
ATOM   4511 O  O    . VAL   B 1 36  ? 45.992 -20.850 -3.597  1.00 11.01 ?  36  VAL   B O    1 
ATOM   4512 C  CB   . VAL   B 1 36  ? 43.107 -19.814 -4.094  1.00 10.36 ?  36  VAL   B CB   1 
ATOM   4513 C  CG1  . VAL   B 1 36  ? 42.602 -20.182 -2.703  1.00 11.19 ?  36  VAL   B CG1  1 
ATOM   4514 C  CG2  . VAL   B 1 36  ? 42.078 -18.977 -4.832  1.00 10.97 ?  36  VAL   B CG2  1 
ATOM   4515 H  H    . VAL   B 1 36  ? 44.802 -19.489 -5.905  1.00 12.13 ?  36  VAL   B H    1 
ATOM   4516 H  HA   . VAL   B 1 36  ? 44.279 -18.193 -3.608  1.00 11.87 ?  36  VAL   B HA   1 
ATOM   4517 H  HB   . VAL   B 1 36  ? 43.234 -20.634 -4.591  1.00 12.41 ?  36  VAL   B HB   1 
ATOM   4518 H  HG11 . VAL   B 1 36  ? 41.665 -20.426 -2.762  1.00 13.41 ?  36  VAL   B HG11 1 
ATOM   4519 H  HG12 . VAL   B 1 36  ? 43.119 -20.924 -2.362  1.00 13.41 ?  36  VAL   B HG12 1 
ATOM   4520 H  HG13 . VAL   B 1 36  ? 42.701 -19.410 -2.118  1.00 13.41 ?  36  VAL   B HG13 1 
ATOM   4521 H  HG21 . VAL   B 1 36  ? 41.233 -19.451 -4.848  1.00 13.15 ?  36  VAL   B HG21 1 
ATOM   4522 H  HG22 . VAL   B 1 36  ? 41.970 -18.127 -4.372  1.00 13.15 ?  36  VAL   B HG22 1 
ATOM   4523 H  HG23 . VAL   B 1 36  ? 42.387 -18.821 -5.739  1.00 13.15 ?  36  VAL   B HG23 1 
ATOM   4524 N  N    . ASN   B 1 37  ? 45.669 -19.323 -1.955  1.00 10.00 ?  37  ASN   B N    1 
ATOM   4525 C  CA   . ASN   B 1 37  ? 46.421 -20.046 -0.943  1.00 10.42 ?  37  ASN   B CA   1 
ATOM   4526 C  C    . ASN   B 1 37  ? 45.475 -20.720 0.042   1.00 10.66 ?  37  ASN   B C    1 
ATOM   4527 O  O    . ASN   B 1 37  ? 44.462 -20.144 0.452   1.00 11.22 ?  37  ASN   B O    1 
ATOM   4528 C  CB   . ASN   B 1 37  ? 47.348 -19.100 -0.186  1.00 10.40 ?  37  ASN   B CB   1 
ATOM   4529 C  CG   . ASN   B 1 37  ? 48.203 -19.818 0.823   1.00 11.00 ?  37  ASN   B CG   1 
ATOM   4530 O  OD1  . ASN   B 1 37  ? 48.540 -20.999 0.653   1.00 11.76 ?  37  ASN   B OD1  1 
ATOM   4531 N  ND2  . ASN   B 1 37  ? 48.549 -19.115 1.895   1.00 11.10 ?  37  ASN   B ND2  1 
ATOM   4532 H  H    . ASN   B 1 37  ? 45.385 -18.551 -1.686  1.00 11.99 ?  37  ASN   B H    1 
ATOM   4533 H  HA   . ASN   B 1 37  ? 46.955 -20.734 -1.362  1.00 12.49 ?  37  ASN   B HA   1 
ATOM   4534 H  HB2  . ASN   B 1 37  ? 47.942 -18.671 -0.819  1.00 12.47 ?  37  ASN   B HB2  1 
ATOM   4535 H  HB3  . ASN   B 1 37  ? 46.823 -18.440 0.285   1.00 12.47 ?  37  ASN   B HB3  1 
ATOM   4536 H  HD21 . ASN   B 1 37  ? 49.044 -19.467 2.505   1.00 13.30 ?  37  ASN   B HD21 1 
ATOM   4537 H  HD22 . ASN   B 1 37  ? 48.299 -18.298 1.979   1.00 13.30 ?  37  ASN   B HD22 1 
ATOM   4538 N  N    . ALA   B 1 38  ? 45.821 -21.957 0.409   1.00 10.95 ?  38  ALA   B N    1 
ATOM   4539 C  CA   . ALA   B 1 38  ? 45.167 -22.701 1.487   1.00 11.40 ?  38  ALA   B CA   1 
ATOM   4540 C  C    . ALA   B 1 38  ? 45.748 -22.212 2.812   1.00 11.13 ?  38  ALA   B C    1 
ATOM   4541 O  O    . ALA   B 1 38  ? 46.654 -22.815 3.397   1.00 11.98 ?  38  ALA   B O    1 
ATOM   4542 C  CB   . ALA   B 1 38  ? 45.388 -24.199 1.307   1.00 12.61 ?  38  ALA   B CB   1 
ATOM   4543 H  H    . ALA   B 1 38  ? 46.465 -22.395 0.049   1.00 13.12 ?  38  ALA   B H    1 
ATOM   4544 H  HA   . ALA   B 1 38  ? 44.214 -22.521 1.483   1.00 13.66 ?  38  ALA   B HA   1 
ATOM   4545 H  HB1  . ALA   B 1 38  ? 44.941 -24.675 2.032   1.00 15.11 ?  38  ALA   B HB1  1 
ATOM   4546 H  HB2  . ALA   B 1 38  ? 45.010 -24.473 0.457   1.00 15.11 ?  38  ALA   B HB2  1 
ATOM   4547 H  HB3  . ALA   B 1 38  ? 46.336 -24.387 1.328   1.00 15.11 ?  38  ALA   B HB3  1 
ATOM   4548 N  N    . ALA   B 1 39  ? 45.232 -21.067 3.271   1.00 10.82 ?  39  ALA   B N    1 
ATOM   4549 C  CA   . ALA   B 1 39  ? 45.785 -20.332 4.398   1.00 11.30 ?  39  ALA   B CA   1 
ATOM   4550 C  C    . ALA   B 1 39  ? 45.171 -20.774 5.725   1.00 11.29 ?  39  ALA   B C    1 
ATOM   4551 O  O    . ALA   B 1 39  ? 44.140 -21.447 5.776   1.00 12.36 ?  39  ALA   B O    1 
ATOM   4552 C  CB   . ALA   B 1 39  ? 45.536 -18.831 4.199   1.00 11.85 ?  39  ALA   B CB   1 
ATOM   4553 H  H    . ALA   B 1 39  ? 44.539 -20.694 2.927   1.00 12.96 ?  39  ALA   B H    1 
ATOM   4554 H  HA   . ALA   B 1 39  ? 46.739 -20.477 4.440   1.00 13.54 ?  39  ALA   B HA   1 
ATOM   4555 H  HB1  . ALA   B 1 39  ? 45.903 -18.345 4.953   1.00 14.20 ?  39  ALA   B HB1  1 
ATOM   4556 H  HB2  . ALA   B 1 39  ? 45.968 -18.545 3.378   1.00 14.20 ?  39  ALA   B HB2  1 
ATOM   4557 H  HB3  . ALA   B 1 39  ? 44.579 -18.672 4.139   1.00 14.20 ?  39  ALA   B HB3  1 
ATOM   4558 N  N    . ASN   B 1 40  ? 45.818 -20.363 6.813   1.00 11.92 ?  40  ASN   B N    1 
ATOM   4559 C  CA   . ASN   B 1 40  ? 45.251 -20.403 8.151   1.00 12.66 ?  40  ASN   B CA   1 
ATOM   4560 C  C    . ASN   B 1 40  ? 45.068 -18.975 8.675   1.00 12.39 ?  40  ASN   B C    1 
ATOM   4561 O  O    . ASN   B 1 40  ? 45.475 -17.993 8.047   1.00 12.37 ?  40  ASN   B O    1 
ATOM   4562 C  CB   . ASN   B 1 40  ? 46.101 -21.274 9.090   1.00 13.79 ?  40  ASN   B CB   1 
ATOM   4563 C  CG   . ASN   B 1 40  ? 47.555 -20.864 9.118   1.00 14.80 ?  40  ASN   B CG   1 
ATOM   4564 O  OD1  . ASN   B 1 40  ? 47.871 -19.681 9.177   1.00 16.58 ?  40  ASN   B OD1  1 
ATOM   4565 N  ND2  . ASN   B 1 40  ? 48.450 -21.838 9.080   1.00 14.52 ?  40  ASN   B ND2  1 
ATOM   4566 H  H    . ASN   B 1 40  ? 46.618 -20.043 6.794   1.00 14.29 ?  40  ASN   B H    1 
ATOM   4567 H  HA   . ASN   B 1 40  ? 44.369 -20.800 8.100   1.00 15.18 ?  40  ASN   B HA   1 
ATOM   4568 H  HB2  . ASN   B 1 40  ? 45.747 -21.199 9.990   1.00 16.53 ?  40  ASN   B HB2  1 
ATOM   4569 H  HB3  . ASN   B 1 40  ? 46.051 -22.193 8.788   1.00 16.53 ?  40  ASN   B HB3  1 
ATOM   4570 H  HD21 . ASN   B 1 40  ? 49.288 -21.652 9.094   1.00 17.41 ?  40  ASN   B HD21 1 
ATOM   4571 H  HD22 . ASN   B 1 40  ? 48.189 -22.656 9.034   1.00 17.41 ?  40  ASN   B HD22 1 
ATOM   4572 N  N    . VAL   B 1 41  ? 44.416 -18.853 9.833   1.00 12.74 ?  41  VAL   B N    1 
ATOM   4573 C  CA   . VAL   B 1 41  ? 43.956 -17.535 10.282  1.00 13.43 ?  41  VAL   B CA   1 
ATOM   4574 C  C    . VAL   B 1 41  ? 45.105 -16.581 10.577  1.00 13.19 ?  41  VAL   B C    1 
ATOM   4575 O  O    . VAL   B 1 41  ? 44.925 -15.360 10.493  1.00 13.53 ?  41  VAL   B O    1 
ATOM   4576 C  CB   . VAL   B 1 41  ? 42.983 -17.614 11.475  1.00 15.22 ?  41  VAL   B CB   1 
ATOM   4577 C  CG1  . VAL   B 1 41  ? 41.680 -18.285 11.067  1.00 15.68 ?  41  VAL   B CG1  1 
ATOM   4578 C  CG2  . VAL   B 1 41  ? 43.634 -18.307 12.670  1.00 16.52 ?  41  VAL   B CG2  1 
ATOM   4579 H  H    . VAL   B 1 41  ? 44.236 -19.496 10.365  1.00 15.28 ?  41  VAL   B H    1 
ATOM   4580 H  HA   . VAL   B 1 41  ? 43.458 -17.135 9.556   1.00 16.10 ?  41  VAL   B HA   1 
ATOM   4581 H  HB   . VAL   B 1 41  ? 42.763 -16.713 11.756  1.00 18.25 ?  41  VAL   B HB   1 
ATOM   4582 H  HG11 . VAL   B 1 41  ? 41.075 -18.291 11.827  1.00 18.79 ?  41  VAL   B HG11 1 
ATOM   4583 H  HG12 . VAL   B 1 41  ? 41.285 -17.786 10.335  1.00 18.79 ?  41  VAL   B HG12 1 
ATOM   4584 H  HG13 . VAL   B 1 41  ? 41.867 -19.194 10.786  1.00 18.79 ?  41  VAL   B HG13 1 
ATOM   4585 H  HG21 . VAL   B 1 41  ? 42.998 -18.341 13.401  1.00 19.81 ?  41  VAL   B HG21 1 
ATOM   4586 H  HG22 . VAL   B 1 41  ? 43.889 -19.208 12.413  1.00 19.81 ?  41  VAL   B HG22 1 
ATOM   4587 H  HG23 . VAL   B 1 41  ? 44.419 -17.805 12.936  1.00 19.81 ?  41  VAL   B HG23 1 
ATOM   4588 N  N    . TYR   B 1 42  ? 46.274 -17.093 10.957  1.00 13.59 ?  42  TYR   B N    1 
ATOM   4589 C  CA   . TYR   B 1 42  ? 47.426 -16.241 11.225  1.00 13.86 ?  42  TYR   B CA   1 
ATOM   4590 C  C    . TYR   B 1 42  ? 48.393 -16.171 10.046  1.00 13.18 ?  42  TYR   B C    1 
ATOM   4591 O  O    . TYR   B 1 42  ? 49.485 -15.608 10.185  1.00 14.48 ?  42  TYR   B O    1 
ATOM   4592 C  CB   . TYR   B 1 42  ? 48.119 -16.650 12.531  1.00 15.50 ?  42  TYR   B CB   1 
ATOM   4593 C  CG   . TYR   B 1 42  ? 47.526 -15.957 13.755  1.00 15.79 ?  42  TYR   B CG   1 
ATOM   4594 C  CD1  . TYR   B 1 42  ? 47.741 -14.601 13.973  1.00 14.79 ?  42  TYR   B CD1  1 
ATOM   4595 C  CD2  . TYR   B 1 42  ? 46.749 -16.648 14.675  1.00 17.33 ?  42  TYR   B CD2  1 
ATOM   4596 C  CE1  . TYR   B 1 42  ? 47.211 -13.953 15.069  1.00 15.98 ?  42  TYR   B CE1  1 
ATOM   4597 C  CE2  . TYR   B 1 42  ? 46.213 -16.004 15.782  1.00 17.75 ?  42  TYR   B CE2  1 
ATOM   4598 C  CZ   . TYR   B 1 42  ? 46.445 -14.652 15.973  1.00 18.05 ?  42  TYR   B CZ   1 
ATOM   4599 O  OH   . TYR   B 1 42  ? 45.924 -13.991 17.069  1.00 20.75 ?  42  TYR   B OH   1 
ATOM   4600 H  H    . TYR   B 1 42  ? 46.426 -17.938 11.055  1.00 16.29 ?  42  TYR   B H    1 
ATOM   4601 H  HA   . TYR   B 1 42  ? 47.100 -15.343 11.357  1.00 16.61 ?  42  TYR   B HA   1 
ATOM   4602 H  HB2  . TYR   B 1 42  ? 48.026 -17.607 12.654  1.00 18.58 ?  42  TYR   B HB2  1 
ATOM   4603 H  HB3  . TYR   B 1 42  ? 49.059 -16.413 12.477  1.00 18.58 ?  42  TYR   B HB3  1 
ATOM   4604 H  HD1  . TYR   B 1 42  ? 48.260 -14.120 13.359  1.00 17.73 ?  42  TYR   B HD1  1 
ATOM   4605 H  HD2  . TYR   B 1 42  ? 46.589 -17.557 14.545  1.00 20.78 ?  42  TYR   B HD2  1 
ATOM   4606 H  HE1  . TYR   B 1 42  ? 47.372 -13.044 15.192  1.00 19.16 ?  42  TYR   B HE1  1 
ATOM   4607 H  HE2  . TYR   B 1 42  ? 45.694 -16.481 16.387  1.00 21.28 ?  42  TYR   B HE2  1 
ATOM   4608 H  HH   . TYR   B 1 42  ? 46.152 -13.187 17.043  1.00 24.89 ?  42  TYR   B HH   1 
ATOM   4609 N  N    . LEU   B 1 43  ? 47.997 -16.687 8.884   1.00 12.34 ?  43  LEU   B N    1 
ATOM   4610 C  CA   . LEU   B 1 43  ? 48.811 -16.617 7.673   1.00 12.06 ?  43  LEU   B CA   1 
ATOM   4611 C  C    . LEU   B 1 43  ? 50.221 -17.125 7.933   1.00 12.36 ?  43  LEU   B C    1 
ATOM   4612 O  O    . LEU   B 1 43  ? 51.204 -16.529 7.490   1.00 13.20 ?  43  LEU   B O    1 
ATOM   4613 C  CB   . LEU   B 1 43  ? 48.831 -15.213 7.064   1.00 12.24 ?  43  LEU   B CB   1 
ATOM   4614 C  CG   . LEU   B 1 43  ? 47.474 -14.599 6.701   1.00 12.53 ?  43  LEU   B CG   1 
ATOM   4615 C  CD1  . LEU   B 1 43  ? 47.693 -13.201 6.123   1.00 13.69 ?  43  LEU   B CD1  1 
ATOM   4616 C  CD2  . LEU   B 1 43  ? 46.704 -15.487 5.736   1.00 12.82 ?  43  LEU   B CD2  1 
ATOM   4617 H  H    . LEU   B 1 43  ? 47.254 -17.098 8.768   1.00 14.79 ?  43  LEU   B H    1 
ATOM   4618 H  HA   . LEU   B 1 43  ? 48.416 -17.210 7.009   1.00 14.45 ?  43  LEU   B HA   1 
ATOM   4619 H  HB2  . LEU   B 1 43  ? 49.261 -14.617 7.696   1.00 14.67 ?  43  LEU   B HB2  1 
ATOM   4620 H  HB3  . LEU   B 1 43  ? 49.357 -15.246 6.248   1.00 14.67 ?  43  LEU   B HB3  1 
ATOM   4621 H  HG   . LEU   B 1 43  ? 46.949 -14.505 7.510   1.00 15.02 ?  43  LEU   B HG   1 
ATOM   4622 H  HD11 . LEU   B 1 43  ? 46.833 -12.814 5.898   1.00 16.41 ?  43  LEU   B HD11 1 
ATOM   4623 H  HD12 . LEU   B 1 43  ? 48.139 -12.649 6.788   1.00 16.41 ?  43  LEU   B HD12 1 
ATOM   4624 H  HD13 . LEU   B 1 43  ? 48.245 -13.269 5.329   1.00 16.41 ?  43  LEU   B HD13 1 
ATOM   4625 H  HD21 . LEU   B 1 43  ? 45.903 -15.019 5.450   1.00 15.37 ?  43  LEU   B HD21 1 
ATOM   4626 H  HD22 . LEU   B 1 43  ? 47.265 -15.681 4.969   1.00 15.37 ?  43  LEU   B HD22 1 
ATOM   4627 H  HD23 . LEU   B 1 43  ? 46.463 -16.310 6.188   1.00 15.37 ?  43  LEU   B HD23 1 
ATOM   4628 N  N    . LYS   B 1 44  ? 50.320 -18.245 8.649   1.00 12.49 ?  44  LYS   B N    1 
ATOM   4629 C  CA   . LYS   B 1 44  ? 51.587 -18.921 8.893   1.00 13.21 ?  44  LYS   B CA   1 
ATOM   4630 C  C    . LYS   B 1 44  ? 51.706 -20.043 7.870   1.00 12.67 ?  44  LYS   B C    1 
ATOM   4631 O  O    . LYS   B 1 44  ? 51.015 -21.061 7.966   1.00 14.05 ?  44  LYS   B O    1 
ATOM   4632 C  CB   . LYS   B 1 44  ? 51.641 -19.434 10.331  1.00 15.12 ?  44  LYS   B CB   1 
ATOM   4633 C  CG   . LYS   B 1 44  ? 51.855 -18.328 11.354  1.00 17.99 ?  44  LYS   B CG   1 
ATOM   4634 C  CD   . LYS   B 1 44  ? 53.041 -17.454 10.929  1.00 21.10 ?  44  LYS   B CD   1 
ATOM   4635 C  CE   . LYS   B 1 44  ? 53.567 -16.576 12.033  1.00 24.09 ?  44  LYS   B CE   1 
ATOM   4636 N  NZ   . LYS   B 1 44  ? 54.746 -15.777 11.618  1.00 25.41 ?  44  LYS   B NZ   1 
ATOM   4637 H  H    . LYS   B 1 44  ? 49.649 -18.636 9.011   1.00 14.97 ?  44  LYS   B H    1 
ATOM   4638 H  HA   . LYS   B 1 44  ? 52.321 -18.309 8.730   1.00 15.84 ?  44  LYS   B HA   1 
ATOM   4639 H  HB2  . LYS   B 1 44  ? 50.797 -19.870 10.542  1.00 18.12 ?  44  LYS   B HB2  1 
ATOM   4640 H  HB3  . LYS   B 1 44  ? 52.369 -20.065 10.418  1.00 18.12 ?  44  LYS   B HB3  1 
ATOM   4641 H  HG2  . LYS   B 1 44  ? 51.063 -17.775 11.411  1.00 21.57 ?  44  LYS   B HG2  1 
ATOM   4642 H  HG3  . LYS   B 1 44  ? 52.059 -18.723 12.221  1.00 21.57 ?  44  LYS   B HG3  1 
ATOM   4643 H  HD2  . LYS   B 1 44  ? 53.758 -18.035 10.615  1.00 25.31 ?  44  LYS   B HD2  1 
ATOM   4644 H  HD3  . LYS   B 1 44  ? 52.750 -16.873 10.207  1.00 25.31 ?  44  LYS   B HD3  1 
ATOM   4645 H  HE2  . LYS   B 1 44  ? 52.873 -15.950 12.266  1.00 28.89 ?  44  LYS   B HE2  1 
ATOM   4646 H  HE3  . LYS   B 1 44  ? 53.810 -17.127 12.795  1.00 28.89 ?  44  LYS   B HE3  1 
ATOM   4647 H  HZ1  . LYS   B 1 44  ? 55.016 -15.264 12.293  1.00 30.48 ?  44  LYS   B HZ1  1 
ATOM   4648 H  HZ2  . LYS   B 1 44  ? 55.412 -16.313 11.374  1.00 30.48 ?  44  LYS   B HZ2  1 
ATOM   4649 H  HZ3  . LYS   B 1 44  ? 54.530 -15.253 10.928  1.00 30.48 ?  44  LYS   B HZ3  1 
ATOM   4650 N  N    . HIS   B 1 45  ? 52.560 -19.831 6.873   1.00 12.44 ?  45  HIS   B N    1 
ATOM   4651 C  CA   . HIS   B 1 45  ? 52.580 -20.664 5.673   1.00 12.48 ?  45  HIS   B CA   1 
ATOM   4652 C  C    . HIS   B 1 45  ? 53.593 -21.792 5.841   1.00 14.46 ?  45  HIS   B C    1 
ATOM   4653 O  O    . HIS   B 1 45  ? 54.649 -21.822 5.217   1.00 16.85 ?  45  HIS   B O    1 
ATOM   4654 C  CB   . HIS   B 1 45  ? 52.892 -19.813 4.453   1.00 12.78 ?  45  HIS   B CB   1 
ATOM   4655 C  CG   . HIS   B 1 45  ? 52.021 -18.609 4.340   1.00 12.28 ?  45  HIS   B CG   1 
ATOM   4656 N  ND1  . HIS   B 1 45  ? 50.644 -18.685 4.305   1.00 12.35 ?  45  HIS   B ND1  1 
ATOM   4657 C  CD2  . HIS   B 1 45  ? 52.339 -17.297 4.257   1.00 12.92 ?  45  HIS   B CD2  1 
ATOM   4658 C  CE1  . HIS   B 1 45  ? 50.156 -17.461 4.201   1.00 12.14 ?  45  HIS   B CE1  1 
ATOM   4659 N  NE2  . HIS   B 1 45  ? 51.161 -16.602 4.168   1.00 12.72 ?  45  HIS   B NE2  1 
ATOM   4660 H  H    . HIS   B 1 45  ? 53.129 -19.188 6.858   1.00 14.92 ?  45  HIS   B H    1 
ATOM   4661 H  HA   . HIS   B 1 45  ? 51.696 -21.056 5.546   1.00 14.96 ?  45  HIS   B HA   1 
ATOM   4662 H  HB2  . HIS   B 1 45  ? 53.809 -19.515 4.504   1.00 15.32 ?  45  HIS   B HB2  1 
ATOM   4663 H  HB3  . HIS   B 1 45  ? 52.762 -20.354 3.654   1.00 15.32 ?  45  HIS   B HB3  1 
ATOM   4664 H  HD2  . HIS   B 1 45  ? 53.197 -16.936 4.261   1.00 15.49 ?  45  HIS   B HD2  1 
ATOM   4665 H  HE1  . HIS   B 1 45  ? 49.255 -17.243 4.150   1.00 14.56 ?  45  HIS   B HE1  1 
ATOM   4666 H  HE2  . HIS   B 1 45  ? 51.087 -15.748 4.110   1.00 15.25 ?  45  HIS   B HE2  1 
ATOM   4667 N  N    . GLY   B 1 46  ? 53.226 -22.750 6.685   1.00 15.62 ?  46  GLY   B N    1 
ATOM   4668 C  CA   . GLY   B 1 46  ? 54.148 -23.807 7.051   1.00 17.44 ?  46  GLY   B CA   1 
ATOM   4669 C  C    . GLY   B 1 46  ? 54.200 -24.997 6.113   1.00 19.05 ?  46  GLY   B C    1 
ATOM   4670 O  O    . GLY   B 1 46  ? 55.277 -25.399 5.662   1.00 22.49 ?  46  GLY   B O    1 
ATOM   4671 H  H    . GLY   B 1 46  ? 52.452 -22.794 7.072   1.00 18.73 ?  46  GLY   B H    1 
ATOM   4672 H  HA2  . GLY   B 1 46  ? 55.038 -23.431 7.109   1.00 20.91 ?  46  GLY   B HA2  1 
ATOM   4673 H  HA3  . GLY   B 1 46  ? 53.906 -24.135 7.932   1.00 20.91 ?  46  GLY   B HA3  1 
ATOM   4674 N  N    . GLY   B 1 47  ? 53.046 -25.581 5.806   1.00 18.35 ?  47  GLY   B N    1 
ATOM   4675 C  CA   . GLY   B 1 47  ? 52.994 -26.871 5.147   1.00 16.44 ?  47  GLY   B CA   1 
ATOM   4676 C  C    . GLY   B 1 47  ? 52.081 -26.855 3.936   1.00 14.35 ?  47  GLY   B C    1 
ATOM   4677 O  O    . GLY   B 1 47  ? 51.424 -25.856 3.644   1.00 14.51 ?  47  GLY   B O    1 
ATOM   4678 H  H    . GLY   B 1 47  ? 52.269 -25.252 5.987   1.00 22.01 ?  47  GLY   B H    1 
ATOM   4679 H  HA2  . GLY   B 1 47  ? 53.882 -27.127 4.858   1.00 19.71 ?  47  GLY   B HA2  1 
ATOM   4680 H  HA3  . GLY   B 1 47  ? 52.670 -27.542 5.773   1.00 19.71 ?  47  GLY   B HA3  1 
ATOM   4681 N  N    . GLY   B 1 48  ? 52.039 -27.999 3.253   1.00 13.57 ?  48  GLY   B N    1 
ATOM   4682 C  CA   . GLY   B 1 48  ? 51.117 -28.149 2.142   1.00 13.22 ?  48  GLY   B CA   1 
ATOM   4683 C  C    . GLY   B 1 48  ? 51.255 -27.040 1.124   1.00 12.72 ?  48  GLY   B C    1 
ATOM   4684 O  O    . GLY   B 1 48  ? 52.357 -26.571 0.816   1.00 13.34 ?  48  GLY   B O    1 
ATOM   4685 H  H    . GLY   B 1 48  ? 52.533 -28.681 3.406   1.00 16.27 ?  48  GLY   B H    1 
ATOM   4686 H  HA2  . GLY   B 1 48  ? 51.281 -28.998 1.700   1.00 15.85 ?  48  GLY   B HA2  1 
ATOM   4687 H  HA3  . GLY   B 1 48  ? 50.206 -28.147 2.473   1.00 15.85 ?  48  GLY   B HA3  1 
ATOM   4688 N  N    . VAL   B 1 49  ? 50.110 -26.610 0.593   1.00 12.64 ?  49  VAL   B N    1 
ATOM   4689 C  CA   . VAL   B 1 49  ? 50.096 -25.587 -0.449  1.00 12.57 ?  49  VAL   B CA   1 
ATOM   4690 C  C    . VAL   B 1 49  ? 50.750 -24.299 0.041   1.00 11.66 ?  49  VAL   B C    1 
ATOM   4691 O  O    . VAL   B 1 49  ? 51.540 -23.677 -0.677  1.00 12.58 ?  49  VAL   B O    1 
ATOM   4692 C  CB   . VAL   B 1 49  ? 48.652 -25.337 -0.932  1.00 13.66 ?  49  VAL   B CB   1 
ATOM   4693 C  CG1  . VAL   B 1 49  ? 48.579 -24.103 -1.822  1.00 13.68 ?  49  VAL   B CG1  1 
ATOM   4694 C  CG2  . VAL   B 1 49  ? 48.107 -26.556 -1.668  1.00 15.19 ?  49  VAL   B CG2  1 
ATOM   4695 H  H    . VAL   B 1 49  ? 49.324 -26.887 0.821   1.00 15.15 ?  49  VAL   B H    1 
ATOM   4696 H  HA   . VAL   B 1 49  ? 50.600 -25.906 -1.211  1.00 15.07 ?  49  VAL   B HA   1 
ATOM   4697 H  HB   . VAL   B 1 49  ? 48.082 -25.180 -0.164  1.00 16.38 ?  49  VAL   B HB   1 
ATOM   4698 H  HG11 . VAL   B 1 49  ? 47.745 -24.119 -2.322  1.00 16.40 ?  49  VAL   B HG11 1 
ATOM   4699 H  HG12 . VAL   B 1 49  ? 48.610 -23.306 -1.268  1.00 16.40 ?  49  VAL   B HG12 1 
ATOM   4700 H  HG13 . VAL   B 1 49  ? 49.328 -24.109 -2.438  1.00 16.40 ?  49  VAL   B HG13 1 
ATOM   4701 H  HG21 . VAL   B 1 49  ? 47.199 -26.374 -1.959  1.00 18.21 ?  49  VAL   B HG21 1 
ATOM   4702 H  HG22 . VAL   B 1 49  ? 48.669 -26.735 -2.441  1.00 18.21 ?  49  VAL   B HG22 1 
ATOM   4703 H  HG23 . VAL   B 1 49  ? 48.117 -27.317 -1.069  1.00 18.21 ?  49  VAL   B HG23 1 
ATOM   4704 N  N    . ALA   B 1 50  ? 50.402 -23.854 1.250   1.00 11.72 ?  50  ALA   B N    1 
ATOM   4705 C  CA   . ALA   B 1 50  ? 50.922 -22.575 1.726   1.00 11.57 ?  50  ALA   B CA   1 
ATOM   4706 C  C    . ALA   B 1 50  ? 52.442 -22.605 1.831   1.00 11.57 ?  50  ALA   B C    1 
ATOM   4707 O  O    . ALA   B 1 50  ? 53.121 -21.642 1.453   1.00 11.86 ?  50  ALA   B O    1 
ATOM   4708 C  CB   . ALA   B 1 50  ? 50.295 -22.212 3.070   1.00 11.81 ?  50  ALA   B CB   1 
ATOM   4709 H  H    . ALA   B 1 50  ? 49.883 -24.263 1.798   1.00 14.05 ?  50  ALA   B H    1 
ATOM   4710 H  HA   . ALA   B 1 50  ? 50.690 -21.884 1.093   1.00 13.86 ?  50  ALA   B HA   1 
ATOM   4711 H  HB1  . ALA   B 1 50  ? 50.655 -21.360 3.366   1.00 14.15 ?  50  ALA   B HB1  1 
ATOM   4712 H  HB2  . ALA   B 1 50  ? 49.334 -22.145 2.961   1.00 14.15 ?  50  ALA   B HB2  1 
ATOM   4713 H  HB3  . ALA   B 1 50  ? 50.509 -22.902 3.717   1.00 14.15 ?  50  ALA   B HB3  1 
ATOM   4714 N  N    . GLY   B 1 51  ? 52.993 -23.697 2.353   1.00 12.21 ?  51  GLY   B N    1 
ATOM   4715 C  CA   . GLY   B 1 51  ? 54.436 -23.803 2.422   1.00 12.98 ?  51  GLY   B CA   1 
ATOM   4716 C  C    . GLY   B 1 51  ? 55.081 -23.751 1.053   1.00 12.69 ?  51  GLY   B C    1 
ATOM   4717 O  O    . GLY   B 1 51  ? 56.122 -23.114 0.871   1.00 13.68 ?  51  GLY   B O    1 
ATOM   4718 H  H    . GLY   B 1 51  ? 52.566 -24.375 2.664   1.00 14.64 ?  51  GLY   B H    1 
ATOM   4719 H  HA2  . GLY   B 1 51  ? 54.793 -23.071 2.953   1.00 15.56 ?  51  GLY   B HA2  1 
ATOM   4720 H  HA3  . GLY   B 1 51  ? 54.686 -24.638 2.848   1.00 15.56 ?  51  GLY   B HA3  1 
ATOM   4721 N  N    . ALA   B 1 52  ? 54.479 -24.423 0.072   1.00 12.54 ?  52  ALA   B N    1 
ATOM   4722 C  CA   . ALA   B 1 52  ? 55.044 -24.425 -1.270  1.00 13.05 ?  52  ALA   B CA   1 
ATOM   4723 C  C    . ALA   B 1 52  ? 54.961 -23.049 -1.921  1.00 12.13 ?  52  ALA   B C    1 
ATOM   4724 O  O    . ALA   B 1 52  ? 55.931 -22.597 -2.548  1.00 12.89 ?  52  ALA   B O    1 
ATOM   4725 C  CB   . ALA   B 1 52  ? 54.352 -25.474 -2.131  1.00 13.50 ?  52  ALA   B CB   1 
ATOM   4726 H  H    . ALA   B 1 52  ? 53.746 -24.868 0.159   1.00 15.03 ?  52  ALA   B H    1 
ATOM   4727 H  HA   . ALA   B 1 52  ? 55.979 -24.661 -1.208  1.00 15.64 ?  52  ALA   B HA   1 
ATOM   4728 H  HB1  . ALA   B 1 52  ? 54.749 -25.460 -3.019  1.00 16.18 ?  52  ALA   B HB1  1 
ATOM   4729 H  HB2  . ALA   B 1 52  ? 54.487 -26.348 -1.727  1.00 16.18 ?  52  ALA   B HB2  1 
ATOM   4730 H  HB3  . ALA   B 1 52  ? 53.410 -25.274 -2.185  1.00 16.18 ?  52  ALA   B HB3  1 
ATOM   4731 N  N    . LEU   B 1 53  ? 53.814 -22.372 -1.802  1.00 11.57 ?  53  LEU   B N    1 
ATOM   4732 C  CA   . LEU   B 1 53  ? 53.702 -21.030 -2.371  1.00 11.80 ?  53  LEU   B CA   1 
ATOM   4733 C  C    . LEU   B 1 53  ? 54.713 -20.092 -1.725  1.00 11.68 ?  53  LEU   B C    1 
ATOM   4734 O  O    . LEU   B 1 53  ? 55.423 -19.349 -2.415  1.00 12.68 ?  53  LEU   B O    1 
ATOM   4735 C  CB   . LEU   B 1 53  ? 52.281 -20.482 -2.200  1.00 12.52 ?  53  LEU   B CB   1 
ATOM   4736 C  CG   . LEU   B 1 53  ? 51.148 -21.209 -2.931  1.00 12.82 ?  53  LEU   B CG   1 
ATOM   4737 C  CD1  . LEU   B 1 53  ? 49.799 -20.604 -2.584  1.00 14.14 ?  53  LEU   B CD1  1 
ATOM   4738 C  CD2  . LEU   B 1 53  ? 51.360 -21.205 -4.440  1.00 14.67 ?  53  LEU   B CD2  1 
ATOM   4739 H  H    . LEU   B 1 53  ? 53.106 -22.656 -1.406  1.00 13.86 ?  53  LEU   B H    1 
ATOM   4740 H  HA   . LEU   B 1 53  ? 53.900 -21.074 -3.323  1.00 14.14 ?  53  LEU   B HA   1 
ATOM   4741 H  HB2  . LEU   B 1 53  ? 52.069 -20.500 -1.257  1.00 15.01 ?  53  LEU   B HB2  1 
ATOM   4742 H  HB3  . LEU   B 1 53  ? 52.278 -19.564 -2.513  1.00 15.01 ?  53  LEU   B HB3  1 
ATOM   4743 H  HG   . LEU   B 1 53  ? 51.133 -22.132 -2.641  1.00 15.36 ?  53  LEU   B HG   1 
ATOM   4744 H  HD11 . LEU   B 1 53  ? 49.103 -21.089 -3.060  1.00 16.95 ?  53  LEU   B HD11 1 
ATOM   4745 H  HD12 . LEU   B 1 53  ? 49.655 -20.682 -1.626  1.00 16.95 ?  53  LEU   B HD12 1 
ATOM   4746 H  HD13 . LEU   B 1 53  ? 49.790 -19.672 -2.845  1.00 16.95 ?  53  LEU   B HD13 1 
ATOM   4747 H  HD21 . LEU   B 1 53  ? 50.639 -21.700 -4.861  1.00 17.59 ?  53  LEU   B HD21 1 
ATOM   4748 H  HD22 . LEU   B 1 53  ? 51.359 -20.289 -4.757  1.00 17.59 ?  53  LEU   B HD22 1 
ATOM   4749 H  HD23 . LEU   B 1 53  ? 52.209 -21.626 -4.643  1.00 17.59 ?  53  LEU   B HD23 1 
ATOM   4750 N  N    . ASN   B 1 54  ? 54.803 -20.119 -0.397  1.00 11.30 ?  54  ASN   B N    1 
ATOM   4751 C  CA   . ASN   B 1 54  ? 55.719 -19.207 0.272   1.00 12.25 ?  54  ASN   B CA   1 
ATOM   4752 C  C    . ASN   B 1 54  ? 57.163 -19.490 -0.126  1.00 12.64 ?  54  ASN   B C    1 
ATOM   4753 O  O    . ASN   B 1 54  ? 57.946 -18.557 -0.352  1.00 13.11 ?  54  ASN   B O    1 
ATOM   4754 C  CB   . ASN   B 1 54  ? 55.563 -19.288 1.783   1.00 12.95 ?  54  ASN   B CB   1 
ATOM   4755 C  CG   . ASN   B 1 54  ? 56.539 -18.371 2.494   1.00 13.21 ?  54  ASN   B CG   1 
ATOM   4756 O  OD1  . ASN   B 1 54  ? 56.561 -17.162 2.249   1.00 13.33 ?  54  ASN   B OD1  1 
ATOM   4757 N  ND2  . ASN   B 1 54  ? 57.381 -18.940 3.347   1.00 14.67 ?  54  ASN   B ND2  1 
ATOM   4758 H  H    . ASN   B 1 54  ? 54.362 -20.645 0.120   1.00 13.54 ?  54  ASN   B H    1 
ATOM   4759 H  HA   . ASN   B 1 54  ? 55.509 -18.302 0.001   1.00 14.69 ?  54  ASN   B HA   1 
ATOM   4760 H  HB2  . ASN   B 1 54  ? 54.661 -19.021 2.028   1.00 15.53 ?  54  ASN   B HB2  1 
ATOM   4761 H  HB3  . ASN   B 1 54  ? 55.732 -20.197 2.077   1.00 15.53 ?  54  ASN   B HB3  1 
ATOM   4762 H  HD21 . ASN   B 1 54  ? 57.958 -18.459 3.769   1.00 17.59 ?  54  ASN   B HD21 1 
ATOM   4763 H  HD22 . ASN   B 1 54  ? 57.350 -19.789 3.485   1.00 17.59 ?  54  ASN   B HD22 1 
ATOM   4764 N  N    . LYS   B 1 55  ? 57.546 -20.769 -0.193  1.00 13.23 ?  55  LYS   B N    1 
ATOM   4765 C  CA   . LYS   B 1 55  ? 58.904 -21.107 -0.609  1.00 14.09 ?  55  LYS   B CA   1 
ATOM   4766 C  C    . LYS   B 1 55  ? 59.199 -20.570 -2.003  1.00 13.86 ?  55  LYS   B C    1 
ATOM   4767 O  O    . LYS   B 1 55  ? 60.300 -20.070 -2.262  1.00 14.75 ?  55  LYS   B O    1 
ATOM   4768 C  CB   . LYS   B 1 55  ? 59.097 -22.623 -0.554  1.00 16.02 ?  55  LYS   B CB   1 
ATOM   4769 C  CG   . LYS   B 1 55  ? 60.458 -23.097 -1.024  1.00 20.06 ?  55  LYS   B CG   1 
ATOM   4770 C  CD   . LYS   B 1 55  ? 60.629 -24.594 -0.818  1.00 23.54 ?  55  LYS   B CD   1 
ATOM   4771 C  CE   . LYS   B 1 55  ? 60.742 -24.955 0.663   1.00 26.58 ?  55  LYS   B CE   1 
ATOM   4772 N  NZ   . LYS   B 1 55  ? 61.113 -26.378 0.868   1.00 28.05 ?  55  LYS   B NZ   1 
ATOM   4773 H  H    . LYS   B 1 55  ? 57.041 -21.441 -0.012  1.00 15.86 ?  55  LYS   B H    1 
ATOM   4774 H  HA   . LYS   B 1 55  ? 59.531 -20.700 0.007   1.00 16.89 ?  55  LYS   B HA   1 
ATOM   4775 H  HB2  . LYS   B 1 55  ? 58.980 -22.909 0.366   1.00 19.21 ?  55  LYS   B HB2  1 
ATOM   4776 H  HB3  . LYS   B 1 55  ? 58.426 -23.042 -1.114  1.00 19.21 ?  55  LYS   B HB3  1 
ATOM   4777 H  HG2  . LYS   B 1 55  ? 60.553 -22.909 -1.971  1.00 24.06 ?  55  LYS   B HG2  1 
ATOM   4778 H  HG3  . LYS   B 1 55  ? 61.148 -22.637 -0.520  1.00 24.06 ?  55  LYS   B HG3  1 
ATOM   4779 H  HD2  . LYS   B 1 55  ? 59.861 -25.061 -1.185  1.00 28.23 ?  55  LYS   B HD2  1 
ATOM   4780 H  HD3  . LYS   B 1 55  ? 61.442 -24.890 -1.261  1.00 28.23 ?  55  LYS   B HD3  1 
ATOM   4781 H  HE2  . LYS   B 1 55  ? 61.423 -24.395 1.071   1.00 31.88 ?  55  LYS   B HE2  1 
ATOM   4782 H  HE3  . LYS   B 1 55  ? 59.884 -24.798 1.091   1.00 31.88 ?  55  LYS   B HE3  1 
ATOM   4783 H  HZ1  . LYS   B 1 55  ? 61.137 -26.560 1.739   1.00 33.64 ?  55  LYS   B HZ1  1 
ATOM   4784 H  HZ2  . LYS   B 1 55  ? 60.513 -26.905 0.478   1.00 33.64 ?  55  LYS   B HZ2  1 
ATOM   4785 H  HZ3  . LYS   B 1 55  ? 61.913 -26.536 0.516   1.00 33.64 ?  55  LYS   B HZ3  1 
ATOM   4786 N  N    . ALA   B 1 56  ? 58.225 -20.658 -2.915  1.00 13.53 ?  56  ALA   B N    1 
ATOM   4787 C  CA   . ALA   B 1 56  ? 58.449 -20.159 -4.267  1.00 14.44 ?  56  ALA   B CA   1 
ATOM   4788 C  C    . ALA   B 1 56  ? 58.728 -18.663 -4.267  1.00 14.15 ?  56  ALA   B C    1 
ATOM   4789 O  O    . ALA   B 1 56  ? 59.453 -18.166 -5.139  1.00 15.24 ?  56  ALA   B O    1 
ATOM   4790 C  CB   . ALA   B 1 56  ? 57.251 -20.485 -5.160  1.00 15.59 ?  56  ALA   B CB   1 
ATOM   4791 H  H    . ALA   B 1 56  ? 57.441 -20.986 -2.777  1.00 16.22 ?  56  ALA   B H    1 
ATOM   4792 H  HA   . ALA   B 1 56  ? 59.225 -20.600 -4.640  1.00 17.32 ?  56  ALA   B HA   1 
ATOM   4793 H  HB1  . ALA   B 1 56  ? 57.425 -20.153 -6.056  1.00 18.69 ?  56  ALA   B HB1  1 
ATOM   4794 H  HB2  . ALA   B 1 56  ? 57.132 -21.448 -5.184  1.00 18.69 ?  56  ALA   B HB2  1 
ATOM   4795 H  HB3  . ALA   B 1 56  ? 56.459 -20.062 -4.798  1.00 18.69 ?  56  ALA   B HB3  1 
ATOM   4796 N  N    . THR   B 1 57  ? 58.169 -17.930 -3.302  1.00 13.83 ?  57  THR   B N    1 
ATOM   4797 C  CA   . THR   B 1 57  ? 58.405 -16.495 -3.187  1.00 13.94 ?  57  THR   B CA   1 
ATOM   4798 C  C    . THR   B 1 57  ? 59.656 -16.162 -2.378  1.00 14.48 ?  57  THR   B C    1 
ATOM   4799 O  O    . THR   B 1 57  ? 59.892 -14.985 -2.078  1.00 15.05 ?  57  THR   B O    1 
ATOM   4800 C  CB   . THR   B 1 57  ? 57.201 -15.763 -2.559  1.00 13.12 ?  57  THR   B CB   1 
ATOM   4801 O  OG1  . THR   B 1 57  ? 57.180 -15.972 -1.141  1.00 13.64 ?  57  THR   B OG1  1 
ATOM   4802 C  CG2  . THR   B 1 57  ? 55.880 -16.186 -3.194  1.00 13.12 ?  57  THR   B CG2  1 
ATOM   4803 H  H    . THR   B 1 57  ? 57.632 -18.242 -2.704  1.00 16.58 ?  57  THR   B H    1 
ATOM   4804 H  HA   . THR   B 1 57  ? 58.525 -16.133 -4.078  1.00 16.71 ?  57  THR   B HA   1 
ATOM   4805 H  HB   . THR   B 1 57  ? 57.305 -14.812 -2.727  1.00 15.73 ?  57  THR   B HB   1 
ATOM   4806 H  HG1  . THR   B 1 57  ? 57.105 -16.792 -0.976  1.00 16.36 ?  57  THR   B HG1  1 
ATOM   4807 H  HG21 . THR   B 1 57  ? 55.156 -15.648 -2.847  1.00 15.73 ?  57  THR   B HG21 1 
ATOM   4808 H  HG22 . THR   B 1 57  ? 55.925 -16.074 -4.158  1.00 15.73 ?  57  THR   B HG22 1 
ATOM   4809 H  HG23 . THR   B 1 57  ? 55.704 -17.120 -2.999  1.00 15.73 ?  57  THR   B HG23 1 
ATOM   4810 N  N    . ASN   B 1 58  ? 60.451 -17.162 -2.014  1.00 15.35 ?  58  ASN   B N    1 
ATOM   4811 C  CA   . ASN   B 1 58  ? 61.646 -16.944 -1.203  1.00 18.23 ?  58  ASN   B CA   1 
ATOM   4812 C  C    . ASN   B 1 58  ? 61.308 -16.231 0.107   1.00 16.13 ?  58  ASN   B C    1 
ATOM   4813 O  O    . ASN   B 1 58  ? 62.047 -15.357 0.572   1.00 16.91 ?  58  ASN   B O    1 
ATOM   4814 C  CB   . ASN   B 1 58  ? 62.736 -16.200 -1.982  1.00 26.06 ?  58  ASN   B CB   1 
ATOM   4815 C  CG   . ASN   B 1 58  ? 64.108 -16.357 -1.355  1.00 35.20 ?  58  ASN   B CG   1 
ATOM   4816 O  OD1  . ASN   B 1 58  ? 64.399 -17.368 -0.717  1.00 37.36 ?  58  ASN   B OD1  1 
ATOM   4817 N  ND2  . ASN   B 1 58  ? 64.958 -15.352 -1.532  1.00 39.45 ?  58  ASN   B ND2  1 
ATOM   4818 H  H    . ASN   B 1 58  ? 60.317 -17.988 -2.223  1.00 18.40 ?  58  ASN   B H    1 
ATOM   4819 H  HA   . ASN   B 1 58  ? 62.008 -17.814 -0.976  1.00 21.86 ?  58  ASN   B HA   1 
ATOM   4820 H  HB2  . ASN   B 1 58  ? 62.776 -16.551 -2.888  1.00 31.25 ?  58  ASN   B HB2  1 
ATOM   4821 H  HB3  . ASN   B 1 58  ? 62.523 -15.255 -2.003  1.00 31.25 ?  58  ASN   B HB3  1 
ATOM   4822 H  HD21 . ASN   B 1 58  ? 65.749 -15.395 -1.197  1.00 47.32 ?  58  ASN   B HD21 1 
ATOM   4823 H  HD22 . ASN   B 1 58  ? 64.717 -14.660 -1.981  1.00 47.32 ?  58  ASN   B HD22 1 
ATOM   4824 N  N    . ASN   B 1 59  ? 60.179 -16.612 0.708   1.00 15.45 ?  59  ASN   B N    1 
ATOM   4825 C  CA   . ASN   B 1 59  ? 59.700 -16.141 2.010   1.00 15.16 ?  59  ASN   B CA   1 
ATOM   4826 C  C    . ASN   B 1 59  ? 59.107 -14.735 1.952   1.00 14.22 ?  59  ASN   B C    1 
ATOM   4827 O  O    . ASN   B 1 59  ? 58.678 -14.227 2.994   1.00 14.35 ?  59  ASN   B O    1 
ATOM   4828 C  CB   . ASN   B 1 59  ? 60.773 -16.191 3.113   1.00 16.27 ?  59  ASN   B CB   1 
ATOM   4829 C  CG   . ASN   B 1 59  ? 60.188 -16.370 4.498   1.00 17.08 ?  59  ASN   B CG   1 
ATOM   4830 O  OD1  . ASN   B 1 59  ? 59.367 -17.260 4.728   1.00 17.24 ?  59  ASN   B OD1  1 
ATOM   4831 N  ND2  . ASN   B 1 59  ? 60.615 -15.532 5.434   1.00 17.62 ?  59  ASN   B ND2  1 
ATOM   4832 H  H    . ASN   B 1 59  ? 59.641 -17.192 0.361   1.00 18.53 ?  59  ASN   B H    1 
ATOM   4833 H  HA   . ASN   B 1 59  ? 58.993 -16.738 2.294   1.00 18.17 ?  59  ASN   B HA   1 
ATOM   4834 H  HB2  . ASN   B 1 59  ? 61.374 -16.936 2.949   1.00 19.51 ?  59  ASN   B HB2  1 
ATOM   4835 H  HB3  . ASN   B 1 59  ? 61.272 -15.359 3.114   1.00 19.51 ?  59  ASN   B HB3  1 
ATOM   4836 H  HD21 . ASN   B 1 59  ? 60.312 -15.596 6.238   1.00 21.13 ?  59  ASN   B HD21 1 
ATOM   4837 H  HD22 . ASN   B 1 59  ? 61.187 -14.924 5.238   1.00 21.13 ?  59  ASN   B HD22 1 
ATOM   4838 N  N    . ALA   B 1 60  ? 59.047 -14.095 0.781   1.00 13.92 ?  60  ALA   B N    1 
ATOM   4839 C  CA   . ALA   B 1 60  ? 58.451 -12.763 0.707   1.00 14.08 ?  60  ALA   B CA   1 
ATOM   4840 C  C    . ALA   B 1 60  ? 56.981 -12.789 1.105   1.00 13.44 ?  60  ALA   B C    1 
ATOM   4841 O  O    . ALA   B 1 60  ? 56.475 -11.836 1.713   1.00 13.79 ?  60  ALA   B O    1 
ATOM   4842 C  CB   . ALA   B 1 60  ? 58.610 -12.184 -0.699  1.00 14.96 ?  60  ALA   B CB   1 
ATOM   4843 H  H    . ALA   B 1 60  ? 59.338 -14.408 0.034   1.00 16.69 ?  60  ALA   B H    1 
ATOM   4844 H  HA   . ALA   B 1 60  ? 58.913 -12.181 1.326   1.00 16.88 ?  60  ALA   B HA   1 
ATOM   4845 H  HB1  . ALA   B 1 60  ? 58.212 -11.303 -0.723  1.00 17.94 ?  60  ALA   B HB1  1 
ATOM   4846 H  HB2  . ALA   B 1 60  ? 59.559 -12.124 -0.908  1.00 17.94 ?  60  ALA   B HB2  1 
ATOM   4847 H  HB3  . ALA   B 1 60  ? 58.171 -12.768 -1.335  1.00 17.94 ?  60  ALA   B HB3  1 
ATOM   4848 N  N    . MET   B 1 61  ? 56.277 -13.869 0.762   1.00 12.63 ?  61  MET   B N    1 
ATOM   4849 C  CA   . MET   B 1 61  ? 54.879 -13.992 1.152   1.00 12.28 ?  61  MET   B CA   1 
ATOM   4850 C  C    . MET   B 1 61  ? 54.735 -13.994 2.672   1.00 12.47 ?  61  MET   B C    1 
ATOM   4851 O  O    . MET   B 1 61  ? 53.834 -13.343 3.220   1.00 12.31 ?  61  MET   B O    1 
ATOM   4852 C  CB   . MET   B 1 61  ? 54.301 -15.262 0.523   1.00 12.12 ?  61  MET   B CB   1 
ATOM   4853 C  CG   . MET   B 1 61  ? 52.860 -15.554 0.946   1.00 12.03 ?  61  MET   B CG   1 
ATOM   4854 S  SD   . MET   B 1 61  ? 52.212 -17.054 0.174   1.00 12.59 ?  61  MET   B SD   1 
ATOM   4855 C  CE   . MET   B 1 61  ? 51.955 -16.463 -1.497  1.00 13.82 ?  61  MET   B CE   1 
ATOM   4856 H  H    . MET   B 1 61  ? 56.581 -14.536 0.300   1.00 15.15 ?  61  MET   B H    1 
ATOM   4857 H  HA   . MET   B 1 61  ? 54.387 -13.242 0.788   1.00 14.72 ?  61  MET   B HA   1 
ATOM   4858 H  HB2  . MET   B 1 61  ? 54.308 -15.169 -0.446  1.00 14.53 ?  61  MET   B HB2  1 
ATOM   4859 H  HB3  . MET   B 1 61  ? 54.845 -16.022 0.781   1.00 14.53 ?  61  MET   B HB3  1 
ATOM   4860 H  HG2  . MET   B 1 61  ? 52.828 -15.682 1.910   1.00 14.42 ?  61  MET   B HG2  1 
ATOM   4861 H  HG3  . MET   B 1 61  ? 52.294 -14.807 0.693   1.00 14.42 ?  61  MET   B HG3  1 
ATOM   4862 H  HE1  . MET   B 1 61  ? 51.563 -17.172 -2.026  1.00 16.56 ?  61  MET   B HE1  1 
ATOM   4863 H  HE2  . MET   B 1 61  ? 51.355 -15.696 -1.475  1.00 16.56 ?  61  MET   B HE2  1 
ATOM   4864 H  HE3  . MET   B 1 61  ? 52.809 -16.198 -1.874  1.00 16.56 ?  61  MET   B HE3  1 
ATOM   4865 N  N    . GLN   B 1 62  ? 55.622 -14.705 3.377   1.00 12.35 ?  62  GLN   B N    1 
ATOM   4866 C  CA   . GLN   B 1 62  ? 55.515 -14.766 4.831   1.00 12.86 ?  62  GLN   B CA   1 
ATOM   4867 C  C    . GLN   B 1 62  ? 55.794 -13.413 5.470   1.00 13.09 ?  62  GLN   B C    1 
ATOM   4868 O  O    . GLN   B 1 62  ? 55.107 -13.022 6.419   1.00 13.54 ?  62  GLN   B O    1 
ATOM   4869 C  CB   . GLN   B 1 62  ? 56.463 -15.824 5.400   1.00 13.31 ?  62  GLN   B CB   1 
ATOM   4870 C  CG   . GLN   B 1 62  ? 56.236 -16.090 6.879   1.00 13.45 ?  62  GLN   B CG   1 
ATOM   4871 C  CD   . GLN   B 1 62  ? 54.860 -16.679 7.125   1.00 13.07 ?  62  GLN   B CD   1 
ATOM   4872 O  OE1  . GLN   B 1 62  ? 54.607 -17.832 6.775   1.00 13.40 ?  62  GLN   B OE1  1 
ATOM   4873 N  NE2  . GLN   B 1 62  ? 53.945 -15.881 7.677   1.00 13.34 ?  62  GLN   B NE2  1 
ATOM   4874 H  H    . GLN   B 1 62  ? 56.281 -15.151 3.039   1.00 14.80 ?  62  GLN   B H    1 
ATOM   4875 H  HA   . GLN   B 1 62  ? 54.609 -15.023 5.059   1.00 15.41 ?  62  GLN   B HA   1 
ATOM   4876 H  HB2  . GLN   B 1 62  ? 56.330 -16.660 4.925   1.00 15.96 ?  62  GLN   B HB2  1 
ATOM   4877 H  HB3  . GLN   B 1 62  ? 57.379 -15.523 5.287   1.00 15.96 ?  62  GLN   B HB3  1 
ATOM   4878 H  HG2  . GLN   B 1 62  ? 56.901 -16.723 7.194   1.00 16.12 ?  62  GLN   B HG2  1 
ATOM   4879 H  HG3  . GLN   B 1 62  ? 56.308 -15.257 7.371   1.00 16.12 ?  62  GLN   B HG3  1 
ATOM   4880 H  HE21 . GLN   B 1 62  ? 54.155 -15.076 7.894   1.00 15.99 ?  62  GLN   B HE21 1 
ATOM   4881 H  HE22 . GLN   B 1 62  ? 53.154 -16.177 7.824   1.00 15.99 ?  62  GLN   B HE22 1 
ATOM   4882 N  N    . VAL   B 1 63  ? 56.810 -12.695 4.982   1.00 13.53 ?  63  VAL   B N    1 
ATOM   4883 C  CA   . VAL   B 1 63  ? 57.113 -11.377 5.537   1.00 14.51 ?  63  VAL   B CA   1 
ATOM   4884 C  C    . VAL   B 1 63  ? 55.921 -10.444 5.351   1.00 13.73 ?  63  VAL   B C    1 
ATOM   4885 O  O    . VAL   B 1 63  ? 55.505 -9.736  6.281   1.00 14.34 ?  63  VAL   B O    1 
ATOM   4886 C  CB   . VAL   B 1 63  ? 58.404 -10.816 4.914   1.00 15.73 ?  63  VAL   B CB   1 
ATOM   4887 C  CG1  . VAL   B 1 63  ? 58.634 -9.378  5.361   1.00 16.44 ?  63  VAL   B CG1  1 
ATOM   4888 C  CG2  . VAL   B 1 63  ? 59.585 -11.695 5.297   1.00 16.22 ?  63  VAL   B CG2  1 
ATOM   4889 H  H    . VAL   B 1 63  ? 57.320 -12.941 4.332   1.00 16.22 ?  63  VAL   B H    1 
ATOM   4890 H  HA   . VAL   B 1 63  ? 57.264 -11.473 6.486   1.00 17.40 ?  63  VAL   B HA   1 
ATOM   4891 H  HB   . VAL   B 1 63  ? 58.328 -10.829 3.946   1.00 18.86 ?  63  VAL   B HB   1 
ATOM   4892 H  HG11 . VAL   B 1 63  ? 59.549 -9.133  5.168   1.00 19.71 ?  63  VAL   B HG11 1 
ATOM   4893 H  HG12 . VAL   B 1 63  ? 58.024 -8.799  4.879   1.00 19.71 ?  63  VAL   B HG12 1 
ATOM   4894 H  HG13 . VAL   B 1 63  ? 58.468 -9.319  6.315   1.00 19.71 ?  63  VAL   B HG13 1 
ATOM   4895 H  HG21 . VAL   B 1 63  ? 60.397 -11.318 4.920   1.00 19.45 ?  63  VAL   B HG21 1 
ATOM   4896 H  HG22 . VAL   B 1 63  ? 59.657 -11.721 6.267   1.00 19.45 ?  63  VAL   B HG22 1 
ATOM   4897 H  HG23 . VAL   B 1 63  ? 59.446 -12.590 4.954   1.00 19.45 ?  63  VAL   B HG23 1 
ATOM   4898 N  N    . GLU   B 1 64  ? 55.350 -10.438 4.146   1.00 12.98 ?  64  GLU   B N    1 
ATOM   4899 C  CA   . GLU   B 1 64  ? 54.186 -9.599  3.869   1.00 13.09 ?  64  GLU   B CA   1 
ATOM   4900 C  C    . GLU   B 1 64  ? 53.000 -9.997  4.742   1.00 12.58 ?  64  GLU   B C    1 
ATOM   4901 O  O    . GLU   B 1 64  ? 52.249 -9.136  5.235   1.00 13.09 ?  64  GLU   B O    1 
ATOM   4902 C  CB   . GLU   B 1 64  ? 53.828 -9.746  2.389   1.00 12.90 ?  64  GLU   B CB   1 
ATOM   4903 C  CG   . GLU   B 1 64  ? 52.569 -9.005  1.948   1.00 13.27 ?  64  GLU   B CG   1 
ATOM   4904 C  CD   . GLU   B 1 64  ? 52.032 -9.506  0.613   1.00 14.06 ?  64  GLU   B CD   1 
ATOM   4905 O  OE1  . GLU   B 1 64  ? 52.206 -10.716 0.306   1.00 14.97 ?  64  GLU   B OE1  1 
ATOM   4906 O  OE2  . GLU   B 1 64  ? 51.419 -8.693  -0.117  1.00 14.69 -1 64  GLU   B OE2  1 
ATOM   4907 H  H    . GLU   B 1 64  ? 55.618 -10.906 3.470   1.00 15.56 ?  64  GLU   B H    1 
ATOM   4908 H  HA   . GLU   B 1 64  ? 54.403 -8.671  4.044   1.00 15.69 ?  64  GLU   B HA   1 
ATOM   4909 H  HB2  . GLU   B 1 64  ? 54.562 -9.395  1.854   1.00 15.46 ?  64  GLU   B HB2  1 
ATOM   4910 H  HB3  . GLU   B 1 64  ? 53.699 -10.681 2.190   1.00 15.46 ?  64  GLU   B HB3  1 
ATOM   4911 H  HG2  . GLU   B 1 64  ? 51.865 -9.126  2.607   1.00 15.91 ?  64  GLU   B HG2  1 
ATOM   4912 H  HG3  . GLU   B 1 64  ? 52.768 -8.058  1.855   1.00 15.91 ?  64  GLU   B HG3  1 
ATOM   4913 N  N    . SER   B 1 65  ? 52.820 -11.304 4.932   1.00 12.21 ?  65  SER   B N    1 
ATOM   4914 C  CA   . SER   B 1 65  ? 51.711 -11.811 5.730   1.00 12.27 ?  65  SER   B CA   1 
ATOM   4915 C  C    . SER   B 1 65  ? 51.842 -11.413 7.192   1.00 12.09 ?  65  SER   B C    1 
ATOM   4916 O  O    . SER   B 1 65  ? 50.843 -11.046 7.828   1.00 12.90 ?  65  SER   B O    1 
ATOM   4917 C  CB   . SER   B 1 65  ? 51.641 -13.334 5.601   1.00 12.54 ?  65  SER   B CB   1 
ATOM   4918 O  OG   . SER   B 1 65  ? 51.281 -13.736 4.287   1.00 12.76 ?  65  SER   B OG   1 
ATOM   4919 H  H    . SER   B 1 65  ? 53.330 -11.922 4.612   1.00 14.64 ?  65  SER   B H    1 
ATOM   4920 H  HA   . SER   B 1 65  ? 50.878 -11.443 5.391   1.00 14.70 ?  65  SER   B HA   1 
ATOM   4921 H  HB2  . SER   B 1 65  ? 52.505 -13.708 5.815   1.00 15.03 ?  65  SER   B HB2  1 
ATOM   4922 H  HB3  . SER   B 1 65  ? 50.972 -13.669 6.224   1.00 15.03 ?  65  SER   B HB3  1 
ATOM   4923 H  HG   . SER   B 1 65  ? 51.843 -13.446 3.731   1.00 15.30 ?  65  SER   B HG   1 
ATOM   4924 N  N    . ASP   B 1 66  ? 53.053 -11.511 7.756   1.00 12.84 ?  66  ASP   B N    1 
ATOM   4925 C  CA   . ASP   B 1 66  ? 53.242 -11.116 9.147   1.00 13.09 ?  66  ASP   B CA   1 
ATOM   4926 C  C    . ASP   B 1 66  ? 52.926 -9.636  9.343   1.00 13.39 ?  66  ASP   B C    1 
ATOM   4927 O  O    . ASP   B 1 66  ? 52.352 -9.245  10.366  1.00 13.78 ?  66  ASP   B O    1 
ATOM   4928 C  CB   . ASP   B 1 66  ? 54.673 -11.423 9.598   1.00 14.51 ?  66  ASP   B CB   1 
ATOM   4929 C  CG   . ASP   B 1 66  ? 54.939 -12.918 9.765   1.00 16.39 ?  66  ASP   B CG   1 
ATOM   4930 O  OD1  . ASP   B 1 66  ? 53.988 -13.730 9.682   1.00 17.01 ?  66  ASP   B OD1  1 
ATOM   4931 O  OD2  . ASP   B 1 66  ? 56.113 -13.284 9.990   1.00 19.05 -1 66  ASP   B OD2  1 
ATOM   4932 H  H    . ASP   B 1 66  ? 53.757 -11.806 7.365   1.00 15.40 ?  66  ASP   B H    1 
ATOM   4933 H  HA   . ASP   B 1 66  ? 52.638 -11.620 9.712   1.00 15.69 ?  66  ASP   B HA   1 
ATOM   4934 H  HB2  . ASP   B 1 66  ? 55.293 -11.086 8.935   1.00 17.40 ?  66  ASP   B HB2  1 
ATOM   4935 H  HB3  . ASP   B 1 66  ? 54.835 -10.989 10.454  1.00 17.40 ?  66  ASP   B HB3  1 
ATOM   4936 N  N    . ASP   B 1 67  ? 53.303 -8.794  8.379   1.00 12.82 ?  67  ASP   B N    1 
ATOM   4937 C  CA   . ASP   B 1 67  ? 52.954 -7.382  8.458   1.00 13.47 ?  67  ASP   B CA   1 
ATOM   4938 C  C    . ASP   B 1 67  ? 51.442 -7.178  8.381   1.00 13.85 ?  67  ASP   B C    1 
ATOM   4939 O  O    . ASP   B 1 67  ? 50.880 -6.371  9.130   1.00 14.30 ?  67  ASP   B O    1 
ATOM   4940 C  CB   . ASP   B 1 67  ? 53.671 -6.614  7.351   1.00 14.90 ?  67  ASP   B CB   1 
ATOM   4941 C  CG   . ASP   B 1 67  ? 53.237 -5.175  7.292   1.00 16.66 ?  67  ASP   B CG   1 
ATOM   4942 O  OD1  . ASP   B 1 67  ? 53.727 -4.359  8.107   1.00 17.73 ?  67  ASP   B OD1  1 
ATOM   4943 O  OD2  . ASP   B 1 67  ? 52.373 -4.876  6.451   1.00 17.75 -1 67  ASP   B OD2  1 
ATOM   4944 H  H    . ASP   B 1 67  ? 53.762 -9.014  7.687   1.00 15.37 ?  67  ASP   B H    1 
ATOM   4945 H  HA   . ASP   B 1 67  ? 53.260 -7.027  9.306   1.00 16.14 ?  67  ASP   B HA   1 
ATOM   4946 H  HB2  . ASP   B 1 67  ? 54.629 -6.642  7.511   1.00 17.87 ?  67  ASP   B HB2  1 
ATOM   4947 H  HB3  . ASP   B 1 67  ? 53.471 -7.032  6.494   1.00 17.87 ?  67  ASP   B HB3  1 
ATOM   4948 N  N    . TYR   B 1 68  ? 50.763 -7.913  7.492   1.00 13.42 ?  68  TYR   B N    1 
ATOM   4949 C  CA   . TYR   B 1 68  ? 49.306 -7.831  7.422   1.00 13.97 ?  68  TYR   B CA   1 
ATOM   4950 C  C    . TYR   B 1 68  ? 48.673 -8.172  8.767   1.00 13.46 ?  68  TYR   B C    1 
ATOM   4951 O  O    . TYR   B 1 68  ? 47.741 -7.495  9.215   1.00 14.55 ?  68  TYR   B O    1 
ATOM   4952 C  CB   . TYR   B 1 68  ? 48.771 -8.759  6.323   1.00 14.66 ?  68  TYR   B CB   1 
ATOM   4953 C  CG   . TYR   B 1 68  ? 47.269 -8.914  6.382   1.00 15.62 ?  68  TYR   B CG   1 
ATOM   4954 C  CD1  . TYR   B 1 68  ? 46.683 -9.873  7.201   1.00 16.59 ?  68  TYR   B CD1  1 
ATOM   4955 C  CD2  . TYR   B 1 68  ? 46.436 -8.076  5.656   1.00 16.87 ?  68  TYR   B CD2  1 
ATOM   4956 C  CE1  . TYR   B 1 68  ? 45.317 -9.996  7.291   1.00 17.69 ?  68  TYR   B CE1  1 
ATOM   4957 C  CE2  . TYR   B 1 68  ? 45.055 -8.206  5.731   1.00 17.48 ?  68  TYR   B CE2  1 
ATOM   4958 C  CZ   . TYR   B 1 68  ? 44.516 -9.163  6.552   1.00 17.94 ?  68  TYR   B CZ   1 
ATOM   4959 O  OH   . TYR   B 1 68  ? 43.149 -9.285  6.643   1.00 19.07 ?  68  TYR   B OH   1 
ATOM   4960 H  H    . TYR   B 1 68  ? 51.122 -8.467  6.932   1.00 16.09 ?  68  TYR   B H    1 
ATOM   4961 H  HA   . TYR   B 1 68  ? 49.059 -6.926  7.196   1.00 16.75 ?  68  TYR   B HA   1 
ATOM   4962 H  HB2  . TYR   B 1 68  ? 48.998 -8.390  5.457   1.00 17.57 ?  68  TYR   B HB2  1 
ATOM   4963 H  HB3  . TYR   B 1 68  ? 49.166 -9.639  6.426   1.00 17.57 ?  68  TYR   B HB3  1 
ATOM   4964 H  HD1  . TYR   B 1 68  ? 47.224 -10.442 7.702   1.00 19.89 ?  68  TYR   B HD1  1 
ATOM   4965 H  HD2  . TYR   B 1 68  ? 46.808 -7.423  5.114   1.00 20.23 ?  68  TYR   B HD2  1 
ATOM   4966 H  HE1  . TYR   B 1 68  ? 44.935 -10.653 7.832   1.00 21.22 ?  68  TYR   B HE1  1 
ATOM   4967 H  HE2  . TYR   B 1 68  ? 44.500 -7.637  5.244   1.00 20.96 ?  68  TYR   B HE2  1 
ATOM   4968 H  HH   . TYR   B 1 68  ? 42.761 -8.726  6.139   1.00 22.87 ?  68  TYR   B HH   1 
ATOM   4969 N  N    . ILE   B 1 69  ? 49.150 -9.241  9.414   1.00 13.29 ?  69  ILE   B N    1 
ATOM   4970 C  CA   . ILE   B 1 69  ? 48.599 -9.665  10.698  1.00 13.95 ?  69  ILE   B CA   1 
ATOM   4971 C  C    . ILE   B 1 69  ? 48.855 -8.618  11.773  1.00 13.86 ?  69  ILE   B C    1 
ATOM   4972 O  O    . ILE   B 1 69  ? 47.984 -8.337  12.602  1.00 14.06 ?  69  ILE   B O    1 
ATOM   4973 C  CB   . ILE   B 1 69  ? 49.177 -11.038 11.089  1.00 14.78 ?  69  ILE   B CB   1 
ATOM   4974 C  CG1  . ILE   B 1 69  ? 48.645 -12.141 10.165  1.00 14.91 ?  69  ILE   B CG1  1 
ATOM   4975 C  CG2  . ILE   B 1 69  ? 48.894 -11.352 12.555  1.00 15.77 ?  69  ILE   B CG2  1 
ATOM   4976 C  CD1  . ILE   B 1 69  ? 47.170 -12.453 10.331  1.00 15.36 ?  69  ILE   B CD1  1 
ATOM   4977 H  H    . ILE   B 1 69  ? 49.796 -9.733  9.134   1.00 15.93 ?  69  ILE   B H    1 
ATOM   4978 H  HA   . ILE   B 1 69  ? 47.639 -9.761  10.607  1.00 16.72 ?  69  ILE   B HA   1 
ATOM   4979 H  HB   . ILE   B 1 69  ? 50.141 -10.996 10.979  1.00 17.72 ?  69  ILE   B HB   1 
ATOM   4980 H  HG12 . ILE   B 1 69  ? 48.787 -11.865 9.246   1.00 17.88 ?  69  ILE   B HG12 1 
ATOM   4981 H  HG13 . ILE   B 1 69  ? 49.141 -12.955 10.341  1.00 17.88 ?  69  ILE   B HG13 1 
ATOM   4982 H  HG21 . ILE   B 1 69  ? 49.033 -12.300 12.704  1.00 18.91 ?  69  ILE   B HG21 1 
ATOM   4983 H  HG22 . ILE   B 1 69  ? 49.501 -10.841 13.115  1.00 18.91 ?  69  ILE   B HG22 1 
ATOM   4984 H  HG23 . ILE   B 1 69  ? 47.976 -11.117 12.758  1.00 18.91 ?  69  ILE   B HG23 1 
ATOM   4985 H  HD11 . ILE   B 1 69  ? 46.934 -13.167 9.721   1.00 18.41 ?  69  ILE   B HD11 1 
ATOM   4986 H  HD12 . ILE   B 1 69  ? 47.005 -12.731 11.245  1.00 18.41 ?  69  ILE   B HD12 1 
ATOM   4987 H  HD13 . ILE   B 1 69  ? 46.652 -11.660 10.126  1.00 18.41 ?  69  ILE   B HD13 1 
ATOM   4988 N  N    . ALA   B 1 70  ? 50.053 -8.035  11.797  1.00 13.92 ?  70  ALA   B N    1 
ATOM   4989 C  CA   . ALA   B 1 70  ? 50.332 -6.998  12.784  1.00 13.46 ?  70  ALA   B CA   1 
ATOM   4990 C  C    . ALA   B 1 70  ? 49.333 -5.854  12.672  1.00 14.06 ?  70  ALA   B C    1 
ATOM   4991 O  O    . ALA   B 1 70  ? 48.892 -5.302  13.685  1.00 14.46 ?  70  ALA   B O    1 
ATOM   4992 C  CB   . ALA   B 1 70  ? 51.757 -6.480  12.606  1.00 14.03 ?  70  ALA   B CB   1 
ATOM   4993 H  H    . ALA   B 1 70  ? 50.695 -8.217  11.266  1.00 16.69 ?  70  ALA   B H    1 
ATOM   4994 H  HA   . ALA   B 1 70  ? 50.259 -7.373  13.675  1.00 16.14 ?  70  ALA   B HA   1 
ATOM   4995 H  HB1  . ALA   B 1 70  ? 51.942 -5.814  13.288  1.00 16.82 ?  70  ALA   B HB1  1 
ATOM   4996 H  HB2  . ALA   B 1 70  ? 52.378 -7.222  12.695  1.00 16.82 ?  70  ALA   B HB2  1 
ATOM   4997 H  HB3  . ALA   B 1 70  ? 51.844 -6.083  11.725  1.00 16.82 ?  70  ALA   B HB3  1 
ATOM   4998 N  N    . THR   B 1 71  ? 48.961 -5.490  11.447  1.00 14.44 ?  71  THR   B N    1 
ATOM   4999 C  CA   . THR   B 1 71  ? 48.062 -4.358  11.236  1.00 15.36 ?  71  THR   B CA   1 
ATOM   5000 C  C    . THR   B 1 71  ? 46.592 -4.728  11.441  1.00 16.24 ?  71  THR   B C    1 
ATOM   5001 O  O    . THR   B 1 71  ? 45.809 -3.911  11.950  1.00 17.51 ?  71  THR   B O    1 
ATOM   5002 C  CB   . THR   B 1 71  ? 48.276 -3.788  9.830   1.00 17.17 ?  71  THR   B CB   1 
ATOM   5003 O  OG1  . THR   B 1 71  ? 49.597 -3.246  9.728   1.00 19.52 ?  71  THR   B OG1  1 
ATOM   5004 C  CG2  . THR   B 1 71  ? 47.254 -2.705  9.507   1.00 18.17 ?  71  THR   B CG2  1 
ATOM   5005 H  H    . THR   B 1 71  ? 49.219 -5.877  10.724  1.00 17.31 ?  71  THR   B H    1 
ATOM   5006 H  HA   . THR   B 1 71  ? 48.283 -3.658  11.870  1.00 18.41 ?  71  THR   B HA   1 
ATOM   5007 H  HB   . THR   B 1 71  ? 48.186 -4.494  9.174   1.00 20.59 ?  71  THR   B HB   1 
ATOM   5008 H  HG1  . THR   B 1 71  ? 49.723 -2.911  8.962   1.00 23.41 ?  71  THR   B HG1  1 
ATOM   5009 H  HG21 . THR   B 1 71  ? 47.556 -2.177  8.748   1.00 21.79 ?  71  THR   B HG21 1 
ATOM   5010 H  HG22 . THR   B 1 71  ? 46.400 -3.106  9.288   1.00 21.79 ?  71  THR   B HG22 1 
ATOM   5011 H  HG23 . THR   B 1 71  ? 47.143 -2.114  10.269  1.00 21.79 ?  71  THR   B HG23 1 
ATOM   5012 N  N    . ASN   B 1 72  ? 46.199 -5.945  11.051  1.00 15.71 ?  72  ASN   B N    1 
ATOM   5013 C  CA   . ASN   B 1 72  ? 44.796 -6.310  10.924  1.00 16.01 ?  72  ASN   B CA   1 
ATOM   5014 C  C    . ASN   B 1 72  ? 44.326 -7.405  11.873  1.00 16.60 ?  72  ASN   B C    1 
ATOM   5015 O  O    . ASN   B 1 72  ? 43.111 -7.563  12.043  1.00 17.82 ?  72  ASN   B O    1 
ATOM   5016 C  CB   . ASN   B 1 72  ? 44.496 -6.742  9.480   1.00 16.76 ?  72  ASN   B CB   1 
ATOM   5017 C  CG   . ASN   B 1 72  ? 44.773 -5.640  8.482   1.00 17.56 ?  72  ASN   B CG   1 
ATOM   5018 O  OD1  . ASN   B 1 72  ? 45.793 -5.645  7.784   1.00 18.83 ?  72  ASN   B OD1  1 
ATOM   5019 N  ND2  . ASN   B 1 72  ? 43.886 -4.666  8.436   1.00 19.35 ?  72  ASN   B ND2  1 
ATOM   5020 H  H    . ASN   B 1 72  ? 46.746 -6.587  10.849  1.00 18.84 ?  72  ASN   B H    1 
ATOM   5021 H  HA   . ASN   B 1 72  ? 44.266 -5.523  11.104  1.00 19.19 ?  72  ASN   B HA   1 
ATOM   5022 H  HB2  . ASN   B 1 72  ? 45.058 -7.499  9.249   1.00 20.10 ?  72  ASN   B HB2  1 
ATOM   5023 H  HB3  . ASN   B 1 72  ? 43.562 -6.983  9.409   1.00 20.10 ?  72  ASN   B HB3  1 
ATOM   5024 H  HD21 . ASN   B 1 72  ? 43.988 -4.011  7.886   1.00 23.20 ?  72  ASN   B HD21 1 
ATOM   5025 H  HD22 . ASN   B 1 72  ? 43.184 -4.694  8.937   1.00 23.20 ?  72  ASN   B HD22 1 
ATOM   5026 N  N    . GLY   B 1 73  ? 45.227 -8.155  12.497  1.00 16.04 ?  73  GLY   B N    1 
ATOM   5027 C  CA   . GLY   B 1 73  ? 44.828 -9.294  13.287  1.00 15.48 ?  73  GLY   B CA   1 
ATOM   5028 C  C    . GLY   B 1 73  ? 44.470 -10.477 12.415  1.00 14.21 ?  73  GLY   B C    1 
ATOM   5029 O  O    . GLY   B 1 73  ? 44.465 -10.394 11.185  1.00 14.17 ?  73  GLY   B O    1 
ATOM   5030 H  H    . GLY   B 1 73  ? 46.078 -8.020  12.475  1.00 19.23 ?  73  GLY   B H    1 
ATOM   5031 H  HA2  . GLY   B 1 73  ? 45.552 -9.547  13.880  1.00 18.56 ?  73  GLY   B HA2  1 
ATOM   5032 H  HA3  . GLY   B 1 73  ? 44.055 -9.058  13.827  1.00 18.56 ?  73  GLY   B HA3  1 
ATOM   5033 N  N    . PRO   B 1 74  ? 44.168 -11.606 13.051  1.00 14.43 ?  74  PRO   B N    1 
ATOM   5034 C  CA   . PRO   B 1 74  ? 43.915 -12.836 12.300  1.00 13.97 ?  74  PRO   B CA   1 
ATOM   5035 C  C    . PRO   B 1 74  ? 42.615 -12.776 11.510  1.00 13.50 ?  74  PRO   B C    1 
ATOM   5036 O  O    . PRO   B 1 74  ? 41.678 -12.033 11.824  1.00 14.84 ?  74  PRO   B O    1 
ATOM   5037 C  CB   . PRO   B 1 74  ? 43.841 -13.903 13.399  1.00 15.01 ?  74  PRO   B CB   1 
ATOM   5038 C  CG   . PRO   B 1 74  ? 43.387 -13.161 14.607  1.00 16.29 ?  74  PRO   B CG   1 
ATOM   5039 C  CD   . PRO   B 1 74  ? 44.038 -11.810 14.503  1.00 15.92 ?  74  PRO   B CD   1 
ATOM   5040 H  HA   . PRO   B 1 74  ? 44.657 -13.025 11.703  1.00 16.75 ?  74  PRO   B HA   1 
ATOM   5041 H  HB2  . PRO   B 1 74  ? 43.199 -14.585 13.146  1.00 18.00 ?  74  PRO   B HB2  1 
ATOM   5042 H  HB3  . PRO   B 1 74  ? 44.719 -14.289 13.538  1.00 18.00 ?  74  PRO   B HB3  1 
ATOM   5043 H  HG2  . PRO   B 1 74  ? 42.419 -13.081 14.593  1.00 19.53 ?  74  PRO   B HG2  1 
ATOM   5044 H  HG3  . PRO   B 1 74  ? 43.681 -13.628 15.403  1.00 19.53 ?  74  PRO   B HG3  1 
ATOM   5045 H  HD2  . PRO   B 1 74  ? 43.465 -11.130 14.900  1.00 19.08 ?  74  PRO   B HD2  1 
ATOM   5046 H  HD3  . PRO   B 1 74  ? 44.912 -11.823 14.920  1.00 19.08 ?  74  PRO   B HD3  1 
ATOM   5047 N  N    . LEU   B 1 75  ? 42.580 -13.595 10.461  1.00 12.85 ?  75  LEU   B N    1 
ATOM   5048 C  CA   . LEU   B 1 75  ? 41.370 -13.806 9.688   1.00 12.93 ?  75  LEU   B CA   1 
ATOM   5049 C  C    . LEU   B 1 75  ? 40.389 -14.659 10.487  1.00 13.25 ?  75  LEU   B C    1 
ATOM   5050 O  O    . LEU   B 1 75  ? 40.722 -15.227 11.528  1.00 14.49 ?  75  LEU   B O    1 
ATOM   5051 C  CB   . LEU   B 1 75  ? 41.692 -14.520 8.374   1.00 13.26 ?  75  LEU   B CB   1 
ATOM   5052 C  CG   . LEU   B 1 75  ? 42.545 -13.770 7.344   1.00 15.11 ?  75  LEU   B CG   1 
ATOM   5053 C  CD1  . LEU   B 1 75  ? 42.740 -14.590 6.066   1.00 16.17 ?  75  LEU   B CD1  1 
ATOM   5054 C  CD2  . LEU   B 1 75  ? 41.960 -12.420 7.016   1.00 18.34 ?  75  LEU   B CD2  1 
ATOM   5055 H  H    . LEU   B 1 75  ? 43.254 -14.053 10.174  1.00 15.41 ?  75  LEU   B H    1 
ATOM   5056 H  HA   . LEU   B 1 75  ? 40.952 -12.956 9.489   1.00 15.50 ?  75  LEU   B HA   1 
ATOM   5057 H  HB2  . LEU   B 1 75  ? 42.163 -15.344 8.586   1.00 15.90 ?  75  LEU   B HB2  1 
ATOM   5058 H  HB3  . LEU   B 1 75  ? 40.853 -14.743 7.937   1.00 15.90 ?  75  LEU   B HB3  1 
ATOM   5059 H  HG   . LEU   B 1 75  ? 43.424 -13.623 7.726   1.00 18.11 ?  75  LEU   B HG   1 
ATOM   5060 H  HD11 . LEU   B 1 75  ? 43.290 -14.082 5.445   1.00 19.39 ?  75  LEU   B HD11 1 
ATOM   5061 H  HD12 . LEU   B 1 75  ? 43.182 -15.425 6.287   1.00 19.39 ?  75  LEU   B HD12 1 
ATOM   5062 H  HD13 . LEU   B 1 75  ? 41.875 -14.768 5.667   1.00 19.39 ?  75  LEU   B HD13 1 
ATOM   5063 H  HD21 . LEU   B 1 75  ? 42.464 -12.028 6.287   1.00 21.99 ?  75  LEU   B HD21 1 
ATOM   5064 H  HD22 . LEU   B 1 75  ? 41.034 -12.534 6.757   1.00 21.99 ?  75  LEU   B HD22 1 
ATOM   5065 H  HD23 . LEU   B 1 75  ? 42.018 -11.854 7.802   1.00 21.99 ?  75  LEU   B HD23 1 
ATOM   5066 N  N    . LYS   B 1 76  ? 39.158 -14.737 9.985   1.00 14.58 ?  76  LYS   B N    1 
ATOM   5067 C  CA   . LYS   B 1 76  ? 38.175 -15.696 10.467  1.00 16.00 ?  76  LYS   B CA   1 
ATOM   5068 C  C    . LYS   B 1 76  ? 38.266 -16.967 9.629   1.00 14.89 ?  76  LYS   B C    1 
ATOM   5069 O  O    . LYS   B 1 76  ? 38.539 -16.914 8.431   1.00 14.47 ?  76  LYS   B O    1 
ATOM   5070 C  CB   . LYS   B 1 76  ? 36.755 -15.135 10.300  1.00 17.90 ?  76  LYS   B CB   1 
ATOM   5071 C  CG   . LYS   B 1 76  ? 36.481 -13.753 10.912  1.00 19.81 ?  76  LYS   B CG   1 
ATOM   5072 C  CD   . LYS   B 1 76  ? 35.076 -13.236 10.551  1.00 21.06 ?  76  LYS   B CD   1 
ATOM   5073 C  CE   . LYS   B 1 76  ? 34.795 -11.870 11.164  1.00 23.03 ?  76  LYS   B CE   1 
ATOM   5074 N  NZ   . LYS   B 1 76  ? 33.508 -11.281 10.697  1.00 23.51 ?  76  LYS   B NZ   1 
ATOM   5075 H  H    . LYS   B 1 76  ? 38.866 -14.240 9.346   1.00 17.48 ?  76  LYS   B H    1 
ATOM   5076 H  HA   . LYS   B 1 76  ? 38.332 -15.914 11.399  1.00 19.18 ?  76  LYS   B HA   1 
ATOM   5077 H  HB2  . LYS   B 1 76  ? 36.565 -15.071 9.351   1.00 21.46 ?  76  LYS   B HB2  1 
ATOM   5078 H  HB3  . LYS   B 1 76  ? 36.133 -15.758 10.709  1.00 21.46 ?  76  LYS   B HB3  1 
ATOM   5079 H  HG2  . LYS   B 1 76  ? 36.546 -13.815 11.878  1.00 23.76 ?  76  LYS   B HG2  1 
ATOM   5080 H  HG3  . LYS   B 1 76  ? 37.136 -13.121 10.573  1.00 23.76 ?  76  LYS   B HG3  1 
ATOM   5081 H  HD2  . LYS   B 1 76  ? 35.007 -13.157 9.586   1.00 25.25 ?  76  LYS   B HD2  1 
ATOM   5082 H  HD3  . LYS   B 1 76  ? 34.414 -13.862 10.883  1.00 25.25 ?  76  LYS   B HD3  1 
ATOM   5083 H  HE2  . LYS   B 1 76  ? 34.752 -11.964 12.128  1.00 27.62 ?  76  LYS   B HE2  1 
ATOM   5084 H  HE3  . LYS   B 1 76  ? 35.511 -11.264 10.919  1.00 27.62 ?  76  LYS   B HE3  1 
ATOM   5085 H  HZ1  . LYS   B 1 76  ? 33.382 -10.486 11.079  1.00 28.20 ?  76  LYS   B HZ1  1 
ATOM   5086 H  HZ2  . LYS   B 1 76  ? 33.522 -11.177 9.813   1.00 28.20 ?  76  LYS   B HZ2  1 
ATOM   5087 H  HZ3  . LYS   B 1 76  ? 32.830 -11.815 10.915  1.00 28.20 ?  76  LYS   B HZ3  1 
ATOM   5088 N  N    . VAL   B 1 77  ? 38.020 -18.119 10.260  1.00 15.38 ?  77  VAL   B N    1 
ATOM   5089 C  CA   . VAL   B 1 77  ? 37.821 -19.333 9.479   1.00 15.64 ?  77  VAL   B CA   1 
ATOM   5090 C  C    . VAL   B 1 77  ? 36.632 -19.107 8.558   1.00 14.24 ?  77  VAL   B C    1 
ATOM   5091 O  O    . VAL   B 1 77  ? 35.563 -18.669 9.000   1.00 14.28 ?  77  VAL   B O    1 
ATOM   5092 C  CB   . VAL   B 1 77  ? 37.619 -20.547 10.398  1.00 17.23 ?  77  VAL   B CB   1 
ATOM   5093 C  CG1  . VAL   B 1 77  ? 37.335 -21.788 9.563   1.00 17.68 ?  77  VAL   B CG1  1 
ATOM   5094 C  CG2  . VAL   B 1 77  ? 38.845 -20.761 11.284  1.00 18.55 ?  77  VAL   B CG2  1 
ATOM   5095 H  H    . VAL   B 1 77  ? 37.964 -18.220 11.108  1.00 18.44 ?  77  VAL   B H    1 
ATOM   5096 H  HA   . VAL   B 1 77  ? 38.598 -19.493 8.926   1.00 18.75 ?  77  VAL   B HA   1 
ATOM   5097 H  HB   . VAL   B 1 77  ? 36.849 -20.386 10.970  1.00 20.67 ?  77  VAL   B HB   1 
ATOM   5098 H  HG11 . VAL   B 1 77  ? 37.384 -22.567 10.138  1.00 21.20 ?  77  VAL   B HG11 1 
ATOM   5099 H  HG12 . VAL   B 1 77  ? 36.443 -21.719 9.181   1.00 21.20 ?  77  VAL   B HG12 1 
ATOM   5100 H  HG13 . VAL   B 1 77  ? 37.994 -21.852 8.858   1.00 21.20 ?  77  VAL   B HG13 1 
ATOM   5101 H  HG21 . VAL   B 1 77  ? 38.708 -21.558 11.817  1.00 22.25 ?  77  VAL   B HG21 1 
ATOM   5102 H  HG22 . VAL   B 1 77  ? 39.623 -20.867 10.718  1.00 22.25 ?  77  VAL   B HG22 1 
ATOM   5103 H  HG23 . VAL   B 1 77  ? 38.952 -19.989 11.860  1.00 22.25 ?  77  VAL   B HG23 1 
ATOM   5104 N  N    . GLY   B 1 78  ? 36.815 -19.386 7.269   1.00 13.89 ?  78  GLY   B N    1 
ATOM   5105 C  CA   . GLY   B 1 78  ? 35.836 -19.068 6.256   1.00 13.34 ?  78  GLY   B CA   1 
ATOM   5106 C  C    . GLY   B 1 78  ? 36.075 -17.749 5.556   1.00 12.61 ?  78  GLY   B C    1 
ATOM   5107 O  O    . GLY   B 1 78  ? 35.389 -17.464 4.569   1.00 13.04 ?  78  GLY   B O    1 
ATOM   5108 H  H    . GLY   B 1 78  ? 37.517 -19.775 6.955   1.00 16.66 ?  78  GLY   B H    1 
ATOM   5109 H  HA2  . GLY   B 1 78  ? 35.831 -19.763 5.585   1.00 15.99 ?  78  GLY   B HA2  1 
ATOM   5110 H  HA3  . GLY   B 1 78  ? 34.956 -19.032 6.665   1.00 15.99 ?  78  GLY   B HA3  1 
ATOM   5111 N  N    . GLY   B 1 79  ? 37.025 -16.943 6.039   1.00 12.77 ?  79  GLY   B N    1 
ATOM   5112 C  CA   . GLY   B 1 79  ? 37.319 -15.649 5.461   1.00 12.58 ?  79  GLY   B CA   1 
ATOM   5113 C  C    . GLY   B 1 79  ? 38.560 -15.668 4.575   1.00 11.89 ?  79  GLY   B C    1 
ATOM   5114 O  O    . GLY   B 1 79  ? 39.177 -16.704 4.328   1.00 12.49 ?  79  GLY   B O    1 
ATOM   5115 H  H    . GLY   B 1 79  ? 37.522 -17.133 6.712   1.00 15.31 ?  79  GLY   B H    1 
ATOM   5116 H  HA2  . GLY   B 1 79  ? 36.567 -15.352 4.923   1.00 15.09 ?  79  GLY   B HA2  1 
ATOM   5117 H  HA3  . GLY   B 1 79  ? 37.464 -15.002 6.167   1.00 15.09 ?  79  GLY   B HA3  1 
ATOM   5118 N  N    . SER   B 1 80  ? 38.922 -14.476 4.095   1.00 12.10 ?  80  SER   B N    1 
ATOM   5119 C  CA   . SER   B 1 80  ? 40.033 -14.344 3.162   1.00 11.75 ?  80  SER   B CA   1 
ATOM   5120 C  C    . SER   B 1 80  ? 40.609 -12.937 3.219   1.00 11.71 ?  80  SER   B C    1 
ATOM   5121 O  O    . SER   B 1 80  ? 39.995 -12.002 3.735   1.00 12.83 ?  80  SER   B O    1 
ATOM   5122 C  CB   . SER   B 1 80  ? 39.595 -14.637 1.722   1.00 12.19 ?  80  SER   B CB   1 
ATOM   5123 O  OG   . SER   B 1 80  ? 38.746 -13.617 1.224   1.00 13.22 ?  80  SER   B OG   1 
ATOM   5124 H  H    . SER   B 1 80  ? 38.544 -13.729 4.295   1.00 14.50 ?  80  SER   B H    1 
ATOM   5125 H  HA   . SER   B 1 80  ? 40.724 -14.975 3.410   1.00 14.09 ?  80  SER   B HA   1 
ATOM   5126 H  HB2  . SER   B 1 80  ? 40.382 -14.685 1.157   1.00 14.62 ?  80  SER   B HB2  1 
ATOM   5127 H  HB3  . SER   B 1 80  ? 39.122 -15.483 1.703   1.00 14.62 ?  80  SER   B HB3  1 
ATOM   5128 H  HG   . SER   B 1 80  ? 38.050 -13.567 1.706   1.00 15.85 ?  80  SER   B HG   1 
ATOM   5129 N  N    . CYS   B 1 81  ? 41.795 -12.796 2.634   1.00 11.49 ?  81  CYS   B N    1 
ATOM   5130 C  CA   . CYS   B 1 81  ? 42.347 -11.485 2.324   1.00 11.47 ?  81  CYS   B CA   1 
ATOM   5131 C  C    . CYS   B 1 81  ? 43.118 -11.566 1.017   1.00 10.73 ?  81  CYS   B C    1 
ATOM   5132 O  O    . CYS   B 1 81  ? 43.623 -12.628 0.643   1.00 11.92 ?  81  CYS   B O    1 
ATOM   5133 C  CB   . CYS   B 1 81  ? 43.246 -10.932 3.441   1.00 12.31 ?  81  CYS   B CB   1 
ATOM   5134 S  SG   . CYS   B 1 81  ? 44.759 -11.868 3.690   1.00 12.82 ?  81  CYS   B SG   1 
ATOM   5135 H  H    . CYS   B 1 81  ? 42.308 -13.453 2.403   1.00 13.77 ?  81  CYS   B H    1 
ATOM   5136 H  HA   . CYS   B 1 81  ? 41.615 -10.860 2.198   1.00 13.75 ?  81  CYS   B HA   1 
ATOM   5137 H  HB2  . CYS   B 1 81  ? 43.498 -10.020 3.221   1.00 14.75 ?  81  CYS   B HB2  1 
ATOM   5138 H  HB3  . CYS   B 1 81  ? 42.748 -10.936 4.277   1.00 14.75 ?  81  CYS   B HB3  1 
ATOM   5139 H  HG   . CYS   B 1 81  ? 45.385 -11.363 4.588   1.00 15.37 ?  81  CYS   B HG   1 
ATOM   5140 N  N    . VAL   B 1 82  ? 43.220 -10.426 0.339   1.00 11.23 ?  82  VAL   B N    1 
ATOM   5141 C  CA   . VAL   B 1 82  ? 43.992 -10.307 -0.896  1.00 11.55 ?  82  VAL   B CA   1 
ATOM   5142 C  C    . VAL   B 1 82  ? 45.336 -9.667  -0.577  1.00 11.66 ?  82  VAL   B C    1 
ATOM   5143 O  O    . VAL   B 1 82  ? 45.391 -8.551  -0.043  1.00 12.73 ?  82  VAL   B O    1 
ATOM   5144 C  CB   . VAL   B 1 82  ? 43.249 -9.469  -1.948  1.00 12.63 ?  82  VAL   B CB   1 
ATOM   5145 C  CG1  . VAL   B 1 82  ? 44.089 -9.327  -3.211  1.00 14.10 ?  82  VAL   B CG1  1 
ATOM   5146 C  CG2  . VAL   B 1 82  ? 41.899 -10.078 -2.260  1.00 13.43 ?  82  VAL   B CG2  1 
ATOM   5147 H  H    . VAL   B 1 82  ? 42.836 -9.689  0.576   1.00 13.46 ?  82  VAL   B H    1 
ATOM   5148 H  HA   . VAL   B 1 82  ? 44.150 -11.188 -1.263  1.00 13.84 ?  82  VAL   B HA   1 
ATOM   5149 H  HB   . VAL   B 1 82  ? 43.097 -8.583  -1.594  1.00 15.15 ?  82  VAL   B HB   1 
ATOM   5150 H  HG11 . VAL   B 1 82  ? 43.527 -8.998  -3.930  1.00 16.90 ?  82  VAL   B HG11 1 
ATOM   5151 H  HG12 . VAL   B 1 82  ? 44.810 -8.697  -3.044  1.00 16.90 ?  82  VAL   B HG12 1 
ATOM   5152 H  HG13 . VAL   B 1 82  ? 44.455 -10.193 -3.449  1.00 16.90 ?  82  VAL   B HG13 1 
ATOM   5153 H  HG21 . VAL   B 1 82  ? 41.469 -9.560  -2.960  1.00 16.10 ?  82  VAL   B HG21 1 
ATOM   5154 H  HG22 . VAL   B 1 82  ? 42.023 -10.995 -2.562  1.00 16.10 ?  82  VAL   B HG22 1 
ATOM   5155 H  HG23 . VAL   B 1 82  ? 41.351 -10.069 -1.459  1.00 16.10 ?  82  VAL   B HG23 1 
ATOM   5156 N  N    . LEU   B 1 83  ? 46.415 -10.358 -0.940  1.00 11.27 ?  83  LEU   B N    1 
ATOM   5157 C  CA   . LEU   B 1 83  ? 47.771 -9.842  -0.825  1.00 11.32 ?  83  LEU   B CA   1 
ATOM   5158 C  C    . LEU   B 1 83  ? 48.471 -9.987  -2.176  1.00 11.22 ?  83  LEU   B C    1 
ATOM   5159 O  O    . LEU   B 1 83  ? 47.867 -10.407 -3.170  1.00 11.17 ?  83  LEU   B O    1 
ATOM   5160 C  CB   . LEU   B 1 83  ? 48.524 -10.515 0.331   1.00 11.71 ?  83  LEU   B CB   1 
ATOM   5161 C  CG   . LEU   B 1 83  ? 48.011 -10.155 1.731   1.00 13.07 ?  83  LEU   B CG   1 
ATOM   5162 C  CD1  . LEU   B 1 83  ? 48.632 -11.034 2.797   1.00 13.46 ?  83  LEU   B CD1  1 
ATOM   5163 C  CD2  . LEU   B 1 83  ? 48.229 -8.675  2.055   1.00 14.24 ?  83  LEU   B CD2  1 
ATOM   5164 H  H    . LEU   B 1 83  ? 46.377 -11.155 -1.269  1.00 13.51 ?  83  LEU   B H    1 
ATOM   5165 H  HA   . LEU   B 1 83  ? 47.720 -8.897  -0.633  1.00 13.56 ?  83  LEU   B HA   1 
ATOM   5166 H  HB2  . LEU   B 1 83  ? 48.454 -11.475 0.228   1.00 14.03 ?  83  LEU   B HB2  1 
ATOM   5167 H  HB3  . LEU   B 1 83  ? 49.457 -10.250 0.281   1.00 14.03 ?  83  LEU   B HB3  1 
ATOM   5168 H  HG   . LEU   B 1 83  ? 47.057 -10.314 1.749   1.00 15.67 ?  83  LEU   B HG   1 
ATOM   5169 H  HD11 . LEU   B 1 83  ? 48.276 -10.778 3.664   1.00 16.14 ?  83  LEU   B HD11 1 
ATOM   5170 H  HD12 . LEU   B 1 83  ? 48.408 -11.961 2.612   1.00 16.14 ?  83  LEU   B HD12 1 
ATOM   5171 H  HD13 . LEU   B 1 83  ? 49.594 -10.918 2.788   1.00 16.14 ?  83  LEU   B HD13 1 
ATOM   5172 H  HD21 . LEU   B 1 83  ? 48.013 -8.523  2.988   1.00 17.07 ?  83  LEU   B HD21 1 
ATOM   5173 H  HD22 . LEU   B 1 83  ? 49.154 -8.446  1.886   1.00 17.07 ?  83  LEU   B HD22 1 
ATOM   5174 H  HD23 . LEU   B 1 83  ? 47.647 -8.140  1.490   1.00 17.07 ?  83  LEU   B HD23 1 
ATOM   5175 N  N    . SER   B 1 84  ? 49.748 -9.617  -2.232  1.00 12.21 ?  84  SER   B N    1 
ATOM   5176 C  CA   . SER   B 1 84  ? 50.479 -9.737  -3.482  1.00 12.42 ?  84  SER   B CA   1 
ATOM   5177 C  C    . SER   B 1 84  ? 50.641 -11.197 -3.888  1.00 11.65 ?  84  SER   B C    1 
ATOM   5178 O  O    . SER   B 1 84  ? 50.751 -12.090 -3.049  1.00 11.61 ?  84  SER   B O    1 
ATOM   5179 C  CB   . SER   B 1 84  ? 51.869 -9.126  -3.334  1.00 14.31 ?  84  SER   B CB   1 
ATOM   5180 O  OG   . SER   B 1 84  ? 52.617 -9.348  -4.513  1.00 15.86 ?  84  SER   B OG   1 
ATOM   5181 H  H    . SER   B 1 84  ? 50.197 -9.289  -1.576  1.00 14.64 ?  84  SER   B H    1 
ATOM   5182 H  HA   . SER   B 1 84  ? 50.007 -9.270  -4.188  1.00 14.89 ?  84  SER   B HA   1 
ATOM   5183 H  HB2  . SER   B 1 84  ? 51.783 -8.168  -3.184  1.00 17.16 ?  84  SER   B HB2  1 
ATOM   5184 H  HB3  . SER   B 1 84  ? 52.324 -9.538  -2.585  1.00 17.16 ?  84  SER   B HB3  1 
ATOM   5185 H  HG   . SER   B 1 84  ? 53.388 -9.003  -4.435  1.00 19.02 ?  84  SER   B HG   1 
ATOM   5186 N  N    . GLY   B 1 85  ? 50.704 -11.427 -5.193  1.00 12.83 ?  85  GLY   B N    1 
ATOM   5187 C  CA   . GLY   B 1 85  ? 51.057 -12.723 -5.723  1.00 13.76 ?  85  GLY   B CA   1 
ATOM   5188 C  C    . GLY   B 1 85  ? 52.526 -12.911 -6.032  1.00 12.84 ?  85  GLY   B C    1 
ATOM   5189 O  O    . GLY   B 1 85  ? 52.903 -13.991 -6.489  1.00 13.20 ?  85  GLY   B O    1 
ATOM   5190 H  H    . GLY   B 1 85  ? 50.557 -10.839 -5.797  1.00 15.38 ?  85  GLY   B H    1 
ATOM   5191 H  HA2  . GLY   B 1 85  ? 50.800 -13.409 -5.085  1.00 16.49 ?  85  GLY   B HA2  1 
ATOM   5192 H  HA3  . GLY   B 1 85  ? 50.567 -12.877 -6.541  1.00 16.49 ?  85  GLY   B HA3  1 
ATOM   5193 N  N    . HIS   B 1 86  ? 53.377 -11.906 -5.819  1.00 12.66 ?  86  HIS   B N    1 
ATOM   5194 C  CA   . HIS   B 1 86  ? 54.839 -12.076 -5.895  1.00 12.58 ?  86  HIS   B CA   1 
ATOM   5195 C  C    . HIS   B 1 86  ? 55.214 -12.589 -7.283  1.00 12.69 ?  86  HIS   B C    1 
ATOM   5196 O  O    . HIS   B 1 86  ? 54.823 -11.978 -8.289  1.00 13.68 ?  86  HIS   B O    1 
ATOM   5197 C  CB   . HIS   B 1 86  ? 55.317 -12.922 -4.717  1.00 13.20 ?  86  HIS   B CB   1 
ATOM   5198 C  CG   . HIS   B 1 86  ? 55.007 -12.310 -3.392  1.00 13.46 ?  86  HIS   B CG   1 
ATOM   5199 N  ND1  . HIS   B 1 86  ? 55.842 -11.402 -2.778  1.00 14.78 ?  86  HIS   B ND1  1 
ATOM   5200 C  CD2  . HIS   B 1 86  ? 53.929 -12.444 -2.583  1.00 13.81 ?  86  HIS   B CD2  1 
ATOM   5201 C  CE1  . HIS   B 1 86  ? 55.288 -11.005 -1.645  1.00 14.51 ?  86  HIS   B CE1  1 
ATOM   5202 N  NE2  . HIS   B 1 86  ? 54.129 -11.622 -1.503  1.00 13.78 ?  86  HIS   B NE2  1 
ATOM   5203 H  H    . HIS   B 1 86  ? 53.133 -11.109 -5.626  1.00 15.17 ?  86  HIS   B H    1 
ATOM   5204 H  HA   . HIS   B 1 86  ? 55.249 -11.204 -5.796  1.00 15.07 ?  86  HIS   B HA   1 
ATOM   5205 H  HB2  . HIS   B 1 86  ? 54.889 -13.791 -4.755  1.00 15.83 ?  86  HIS   B HB2  1 
ATOM   5206 H  HB3  . HIS   B 1 86  ? 56.282 -13.027 -4.773  1.00 15.83 ?  86  HIS   B HB3  1 
ATOM   5207 H  HD2  . HIS   B 1 86  ? 53.181 -12.981 -2.738  1.00 16.55 ?  86  HIS   B HD2  1 
ATOM   5208 H  HE1  . HIS   B 1 86  ? 55.661 -10.408 -1.040  1.00 17.39 ?  86  HIS   B HE1  1 
ATOM   5209 H  HE2  . HIS   B 1 86  ? 53.588 -11.530 -0.837  1.00 16.52 ?  86  HIS   B HE2  1 
ATOM   5210 N  N    . ASN   B 1 87  ? 55.984 -13.672 -7.389  1.00 13.43 ?  87  ASN   B N    1 
ATOM   5211 C  CA   . ASN   B 1 87  ? 56.378 -14.244 -8.668  1.00 13.99 ?  87  ASN   B CA   1 
ATOM   5212 C  C    . ASN   B 1 87  ? 55.391 -15.286 -9.172  1.00 13.95 ?  87  ASN   B C    1 
ATOM   5213 O  O    . ASN   B 1 87  ? 55.705 -15.997 -10.134 1.00 15.74 ?  87  ASN   B O    1 
ATOM   5214 C  CB   . ASN   B 1 87  ? 57.770 -14.875 -8.552  1.00 15.83 ?  87  ASN   B CB   1 
ATOM   5215 C  CG   . ASN   B 1 87  ? 57.824 -15.987 -7.511  1.00 16.73 ?  87  ASN   B CG   1 
ATOM   5216 O  OD1  . ASN   B 1 87  ? 57.186 -15.904 -6.459  1.00 16.04 ?  87  ASN   B OD1  1 
ATOM   5217 N  ND2  . ASN   B 1 87  ? 58.567 -17.051 -7.817  1.00 19.03 ?  87  ASN   B ND2  1 
ATOM   5218 H  H    . ASN   B 1 87  ? 56.296 -14.103 -6.715  1.00 16.09 ?  87  ASN   B H    1 
ATOM   5219 H  HA   . ASN   B 1 87  ? 56.423 -13.537 -9.328  1.00 16.77 ?  87  ASN   B HA   1 
ATOM   5220 H  HB2  . ASN   B 1 87  ? 58.016 -15.252 -9.412  1.00 18.98 ?  87  ASN   B HB2  1 
ATOM   5221 H  HB3  . ASN   B 1 87  ? 58.404 -14.189 -8.296  1.00 18.98 ?  87  ASN   B HB3  1 
ATOM   5222 H  HD21 . ASN   B 1 87  ? 58.630 -17.702 -7.263  1.00 22.82 ?  87  ASN   B HD21 1 
ATOM   5223 H  HD22 . ASN   B 1 87  ? 58.991 -17.078 -8.566  1.00 22.82 ?  87  ASN   B HD22 1 
ATOM   5224 N  N    . LEU   B 1 88  ? 54.210 -15.385 -8.553  1.00 12.84 ?  88  LEU   B N    1 
ATOM   5225 C  CA   . LEU   B 1 88  ? 53.228 -16.415 -8.877  1.00 13.05 ?  88  LEU   B CA   1 
ATOM   5226 C  C    . LEU   B 1 88  ? 51.998 -15.896 -9.602  1.00 12.86 ?  88  LEU   B C    1 
ATOM   5227 O  O    . LEU   B 1 88  ? 51.400 -16.645 -10.387 1.00 14.66 ?  88  LEU   B O    1 
ATOM   5228 C  CB   . LEU   B 1 88  ? 52.756 -17.099 -7.592  1.00 14.06 ?  88  LEU   B CB   1 
ATOM   5229 C  CG   . LEU   B 1 88  ? 53.870 -17.770 -6.799  1.00 16.33 ?  88  LEU   B CG   1 
ATOM   5230 C  CD1  . LEU   B 1 88  ? 53.371 -18.165 -5.419  1.00 18.27 ?  88  LEU   B CD1  1 
ATOM   5231 C  CD2  . LEU   B 1 88  ? 54.381 -18.978 -7.559  1.00 19.50 ?  88  LEU   B CD2  1 
ATOM   5232 H  H    . LEU   B 1 88  ? 53.952 -14.853 -7.920  1.00 15.40 ?  88  LEU   B H    1 
ATOM   5233 H  HA   . LEU   B 1 88  ? 53.642 -17.079 -9.437  1.00 15.64 ?  88  LEU   B HA   1 
ATOM   5234 H  HB2  . LEU   B 1 88  ? 52.339 -16.441 -7.014  1.00 16.85 ?  88  LEU   B HB2  1 
ATOM   5235 H  HB3  . LEU   B 1 88  ? 52.106 -17.785 -7.825  1.00 16.85 ?  88  LEU   B HB3  1 
ATOM   5236 H  HG   . LEU   B 1 88  ? 54.602 -17.147 -6.689  1.00 19.57 ?  88  LEU   B HG   1 
ATOM   5237 H  HD11 . LEU   B 1 88  ? 54.002 -18.784 -5.020  1.00 21.91 ?  88  LEU   B HD11 1 
ATOM   5238 H  HD12 . LEU   B 1 88  ? 53.293 -17.369 -4.872  1.00 21.91 ?  88  LEU   B HD12 1 
ATOM   5239 H  HD13 . LEU   B 1 88  ? 52.504 -18.590 -5.511  1.00 21.91 ?  88  LEU   B HD13 1 
ATOM   5240 H  HD21 . LEU   B 1 88  ? 55.013 -19.456 -7.000  1.00 23.38 ?  88  LEU   B HD21 1 
ATOM   5241 H  HD22 . LEU   B 1 88  ? 53.633 -19.553 -7.780  1.00 23.38 ?  88  LEU   B HD22 1 
ATOM   5242 H  HD23 . LEU   B 1 88  ? 54.821 -18.678 -8.370  1.00 23.38 ?  88  LEU   B HD23 1 
ATOM   5243 N  N    . ALA   B 1 89  ? 51.591 -14.660 -9.332  1.00 12.11 ?  89  ALA   B N    1 
ATOM   5244 C  CA   . ALA   B 1 89  ? 50.300 -14.160 -9.780  1.00 11.66 ?  89  ALA   B CA   1 
ATOM   5245 C  C    . ALA   B 1 89  ? 50.273 -12.670 -9.496  1.00 12.14 ?  89  ALA   B C    1 
ATOM   5246 O  O    . ALA   B 1 89  ? 51.109 -12.153 -8.755  1.00 12.96 ?  89  ALA   B O    1 
ATOM   5247 C  CB   . ALA   B 1 89  ? 49.158 -14.839 -9.026  1.00 12.00 ?  89  ALA   B CB   1 
ATOM   5248 H  H    . ALA   B 1 89  ? 52.037 -14.084 -8.877  1.00 14.52 ?  89  ALA   B H    1 
ATOM   5249 H  HA   . ALA   B 1 89  ? 50.185 -14.306 -10.734 1.00 13.97 ?  89  ALA   B HA   1 
ATOM   5250 H  HB1  . ALA   B 1 89  ? 48.309 -14.501 -9.362  1.00 14.38 ?  89  ALA   B HB1  1 
ATOM   5251 H  HB2  . ALA   B 1 89  ? 49.209 -15.797 -9.177  1.00 14.38 ?  89  ALA   B HB2  1 
ATOM   5252 H  HB3  . ALA   B 1 89  ? 49.242 -14.646 -8.084  1.00 14.38 ?  89  ALA   B HB3  1 
ATOM   5253 N  N    . LYS   B 1 90  ? 49.284 -11.980 -10.060 1.00 13.10 ?  90  LYS   B N    1 
ATOM   5254 C  CA   . LYS   B 1 90  ? 49.097 -10.591 -9.655  1.00 13.20 ?  90  LYS   B CA   1 
ATOM   5255 C  C    . LYS   B 1 90  ? 48.780 -10.516 -8.165  1.00 12.89 ?  90  LYS   B C    1 
ATOM   5256 O  O    . LYS   B 1 90  ? 49.427 -9.769  -7.416  1.00 13.91 ?  90  LYS   B O    1 
ATOM   5257 C  CB   . LYS   B 1 90  ? 48.025 -9.922  -10.517 1.00 14.52 ?  90  LYS   B CB   1 
ATOM   5258 C  CG   . LYS   B 1 90  ? 47.720 -8.490  -10.125 1.00 15.26 ?  90  LYS   B CG   1 
ATOM   5259 C  CD   . LYS   B 1 90  ? 48.932 -7.593  -10.180 1.00 17.88 ?  90  LYS   B CD   1 
ATOM   5260 C  CE   . LYS   B 1 90  ? 48.491 -6.171  -9.918  1.00 19.94 ?  90  LYS   B CE   1 
ATOM   5261 N  NZ   . LYS   B 1 90  ? 49.643 -5.238  -9.828  1.00 19.67 ?  90  LYS   B NZ   1 
ATOM   5262 H  H    . LYS   B 1 90  ? 48.733 -12.280 -10.650 1.00 15.71 ?  90  LYS   B H    1 
ATOM   5263 H  HA   . LYS   B 1 90  ? 49.924 -10.119 -9.803  1.00 15.83 ?  90  LYS   B HA   1 
ATOM   5264 H  HB2  . LYS   B 1 90  ? 48.325 -9.916  -11.443 1.00 17.40 ?  90  LYS   B HB2  1 
ATOM   5265 H  HB3  . LYS   B 1 90  ? 47.200 -10.431 -10.450 1.00 17.40 ?  90  LYS   B HB3  1 
ATOM   5266 H  HG2  . LYS   B 1 90  ? 47.054 -8.131  -10.735 1.00 18.30 ?  90  LYS   B HG2  1 
ATOM   5267 H  HG3  . LYS   B 1 90  ? 47.372 -8.475  -9.218  1.00 18.30 ?  90  LYS   B HG3  1 
ATOM   5268 H  HD2  . LYS   B 1 90  ? 49.566 -7.852  -9.493  1.00 21.44 ?  90  LYS   B HD2  1 
ATOM   5269 H  HD3  . LYS   B 1 90  ? 49.337 -7.640  -11.059 1.00 21.44 ?  90  LYS   B HD3  1 
ATOM   5270 H  HE2  . LYS   B 1 90  ? 47.922 -5.868  -10.646 1.00 23.91 ?  90  LYS   B HE2  1 
ATOM   5271 H  HE3  . LYS   B 1 90  ? 48.008 -6.126  -9.079  1.00 23.91 ?  90  LYS   B HE3  1 
ATOM   5272 H  HZ1  . LYS   B 1 90  ? 49.359 -4.407  -9.677  1.00 23.59 ?  90  LYS   B HZ1  1 
ATOM   5273 H  HZ2  . LYS   B 1 90  ? 50.183 -5.483  -9.164  1.00 23.59 ?  90  LYS   B HZ2  1 
ATOM   5274 H  HZ3  . LYS   B 1 90  ? 50.105 -5.247  -10.591 1.00 23.59 ?  90  LYS   B HZ3  1 
ATOM   5275 N  N    . HIS   B 1 91  ? 47.817 -11.328 -7.717  1.00 11.85 ?  91  HIS   B N    1 
ATOM   5276 C  CA   . HIS   B 1 91  ? 47.356 -11.354 -6.343  1.00 11.68 ?  91  HIS   B CA   1 
ATOM   5277 C  C    . HIS   B 1 91  ? 47.352 -12.782 -5.829  1.00 10.82 ?  91  HIS   B C    1 
ATOM   5278 O  O    . HIS   B 1 91  ? 47.125 -13.734 -6.585  1.00 11.51 ?  91  HIS   B O    1 
ATOM   5279 C  CB   . HIS   B 1 91  ? 45.904 -10.871 -6.226  1.00 13.16 ?  91  HIS   B CB   1 
ATOM   5280 C  CG   . HIS   B 1 91  ? 45.693 -9.462  -6.664  1.00 16.46 ?  91  HIS   B CG   1 
ATOM   5281 N  ND1  . HIS   B 1 91  ? 46.290 -8.385  -6.044  1.00 18.88 ?  91  HIS   B ND1  1 
ATOM   5282 C  CD2  . HIS   B 1 91  ? 44.914 -8.948  -7.643  1.00 18.76 ?  91  HIS   B CD2  1 
ATOM   5283 C  CE1  . HIS   B 1 91  ? 45.907 -7.268  -6.637  1.00 19.76 ?  91  HIS   B CE1  1 
ATOM   5284 N  NE2  . HIS   B 1 91  ? 45.066 -7.582  -7.607  1.00 20.02 ?  91  HIS   B NE2  1 
ATOM   5285 H  H    . HIS   B 1 91  ? 47.399 -11.893 -8.215  1.00 14.21 ?  91  HIS   B H    1 
ATOM   5286 H  HA   . HIS   B 1 91  ? 47.928 -10.796 -5.780  1.00 14.00 ?  91  HIS   B HA   1 
ATOM   5287 H  HB2  . HIS   B 1 91  ? 45.341 -11.435 -6.774  1.00 15.77 ?  91  HIS   B HB2  1 
ATOM   5288 H  HB3  . HIS   B 1 91  ? 45.625 -10.933 -5.296  1.00 15.77 ?  91  HIS   B HB3  1 
ATOM   5289 H  HD1  . HIS   B 1 91  ? 46.835 -8.431  -5.378  1.00 22.64 ?  91  HIS   B HD1  1 
ATOM   5290 H  HD2  . HIS   B 1 91  ? 44.381 -9.420  -8.237  1.00 22.50 ?  91  HIS   B HD2  1 
ATOM   5291 H  HE1  . HIS   B 1 91  ? 46.178 -6.406  -6.404  1.00 23.69 ?  91  HIS   B HE1  1 
ATOM   5292 N  N    . CYS   B 1 92  ? 47.538 -12.914 -4.524  1.00 10.83 ?  92  CYS   B N    1 
ATOM   5293 C  CA   . CYS   B 1 92  ? 47.237 -14.151 -3.817  1.00 10.51 ?  92  CYS   B CA   1 
ATOM   5294 C  C    . CYS   B 1 92  ? 46.018 -13.918 -2.935  1.00 10.07 ?  92  CYS   B C    1 
ATOM   5295 O  O    . CYS   B 1 92  ? 46.014 -13.006 -2.096  1.00 11.43 ?  92  CYS   B O    1 
ATOM   5296 C  CB   . CYS   B 1 92  ? 48.412 -14.607 -2.959  1.00 11.03 ?  92  CYS   B CB   1 
ATOM   5297 S  SG   . CYS   B 1 92  ? 48.057 -16.147 -2.061  1.00 11.00 ?  92  CYS   B SG   1 
ATOM   5298 H  H    . CYS   B 1 92  ? 47.858 -12.291 -4.013  1.00 12.98 ?  92  CYS   B H    1 
ATOM   5299 H  HA   . CYS   B 1 92  ? 47.037 -14.847 -4.463  1.00 12.60 ?  92  CYS   B HA   1 
ATOM   5300 H  HB2  . CYS   B 1 92  ? 49.179 -14.753 -3.526  1.00 13.22 ?  92  CYS   B HB2  1 
ATOM   5301 H  HB3  . CYS   B 1 92  ? 48.603 -13.913 -2.306  1.00 13.22 ?  92  CYS   B HB3  1 
ATOM   5302 H  HG   . CYS   B 1 92  ? 49.032 -16.455 -1.426  1.00 13.19 ?  92  CYS   B HG   1 
ATOM   5303 N  N    . LEU   B 1 93  ? 44.980 -14.727 -3.142  1.00 10.18 ?  93  LEU   B N    1 
ATOM   5304 C  CA   . LEU   B 1 93  ? 43.803 -14.731 -2.283  1.00 10.23 ?  93  LEU   B CA   1 
ATOM   5305 C  C    . LEU   B 1 93  ? 44.024 -15.795 -1.215  1.00 9.82  ?  93  LEU   B C    1 
ATOM   5306 O  O    . LEU   B 1 93  ? 43.980 -16.996 -1.508  1.00 10.71 ?  93  LEU   B O    1 
ATOM   5307 C  CB   . LEU   B 1 93  ? 42.542 -15.026 -3.092  1.00 10.75 ?  93  LEU   B CB   1 
ATOM   5308 C  CG   . LEU   B 1 93  ? 41.248 -15.035 -2.280  1.00 11.49 ?  93  LEU   B CG   1 
ATOM   5309 C  CD1  . LEU   B 1 93  ? 40.902 -13.642 -1.795  1.00 12.00 ?  93  LEU   B CD1  1 
ATOM   5310 C  CD2  . LEU   B 1 93  ? 40.118 -15.630 -3.101  1.00 11.99 ?  93  LEU   B CD2  1 
ATOM   5311 H  H    . LEU   B 1 93  ? 44.940 -15.309 -3.785  1.00 12.20 ?  93  LEU   B H    1 
ATOM   5312 H  HA   . LEU   B 1 93  ? 43.713 -13.868 -1.855  1.00 12.26 ?  93  LEU   B HA   1 
ATOM   5313 H  HB2  . LEU   B 1 93  ? 42.451 -14.338 -3.776  1.00 12.89 ?  93  LEU   B HB2  1 
ATOM   5314 H  HB3  . LEU   B 1 93  ? 42.634 -15.889 -3.510  1.00 12.89 ?  93  LEU   B HB3  1 
ATOM   5315 H  HG   . LEU   B 1 93  ? 41.369 -15.594 -1.502  1.00 13.78 ?  93  LEU   B HG   1 
ATOM   5316 H  HD11 . LEU   B 1 93  ? 40.046 -13.666 -1.345  1.00 14.38 ?  93  LEU   B HD11 1 
ATOM   5317 H  HD12 . LEU   B 1 93  ? 41.592 -13.341 -1.183  1.00 14.38 ?  93  LEU   B HD12 1 
ATOM   5318 H  HD13 . LEU   B 1 93  ? 40.857 -13.043 -2.560  1.00 14.38 ?  93  LEU   B HD13 1 
ATOM   5319 H  HD21 . LEU   B 1 93  ? 39.303 -15.622 -2.570  1.00 14.37 ?  93  LEU   B HD21 1 
ATOM   5320 H  HD22 . LEU   B 1 93  ? 39.992 -15.099 -3.903  1.00 14.37 ?  93  LEU   B HD22 1 
ATOM   5321 H  HD23 . LEU   B 1 93  ? 40.345 -16.542 -3.340  1.00 14.37 ?  93  LEU   B HD23 1 
ATOM   5322 N  N    . HIS   B 1 94  ? 44.301 -15.359 0.007   1.00 10.08 ?  94  HIS   B N    1 
ATOM   5323 C  CA   . HIS   B 1 94  ? 44.519 -16.264 1.128   1.00 10.15 ?  94  HIS   B CA   1 
ATOM   5324 C  C    . HIS   B 1 94  ? 43.161 -16.616 1.713   1.00 10.79 ?  94  HIS   B C    1 
ATOM   5325 O  O    . HIS   B 1 94  ? 42.493 -15.738 2.265   1.00 12.01 ?  94  HIS   B O    1 
ATOM   5326 C  CB   . HIS   B 1 94  ? 45.390 -15.583 2.182   1.00 10.69 ?  94  HIS   B CB   1 
ATOM   5327 C  CG   . HIS   B 1 94  ? 46.774 -15.284 1.714   1.00 10.65 ?  94  HIS   B CG   1 
ATOM   5328 N  ND1  . HIS   B 1 94  ? 47.802 -16.197 1.800   1.00 11.02 ?  94  HIS   B ND1  1 
ATOM   5329 C  CD2  . HIS   B 1 94  ? 47.284 -14.178 1.118   1.00 11.04 ?  94  HIS   B CD2  1 
ATOM   5330 C  CE1  . HIS   B 1 94  ? 48.892 -15.647 1.294   1.00 10.96 ?  94  HIS   B CE1  1 
ATOM   5331 N  NE2  . HIS   B 1 94  ? 48.607 -14.427 0.873   1.00 11.16 ?  94  HIS   B NE2  1 
ATOM   5332 H  H    . HIS   B 1 94  ? 44.380 -14.523 0.211   1.00 12.08 ?  94  HIS   B H    1 
ATOM   5333 H  HA   . HIS   B 1 94  ? 44.956 -17.073 0.820   1.00 12.16 ?  94  HIS   B HA   1 
ATOM   5334 H  HB2  . HIS   B 1 94  ? 44.975 -14.748 2.435   1.00 12.81 ?  94  HIS   B HB2  1 
ATOM   5335 H  HB3  . HIS   B 1 94  ? 45.459 -16.170 2.948   1.00 12.81 ?  94  HIS   B HB3  1 
ATOM   5336 H  HD2  . HIS   B 1 94  ? 46.829 -13.394 0.918   1.00 13.23 ?  94  HIS   B HD2  1 
ATOM   5337 H  HE1  . HIS   B 1 94  ? 49.720 -16.067 1.238   1.00 13.14 ?  94  HIS   B HE1  1 
ATOM   5338 H  HE2  . HIS   B 1 94  ? 49.165 -13.890 0.506   1.00 13.37 ?  94  HIS   B HE2  1 
ATOM   5339 N  N    . VAL   B 1 95  ? 42.726 -17.870 1.563   1.00 10.51 ?  95  VAL   B N    1 
ATOM   5340 C  CA   . VAL   B 1 95  ? 41.396 -18.306 1.991   1.00 10.65 ?  95  VAL   B CA   1 
ATOM   5341 C  C    . VAL   B 1 95  ? 41.561 -19.343 3.087   1.00 10.72 ?  95  VAL   B C    1 
ATOM   5342 O  O    . VAL   B 1 95  ? 42.336 -20.294 2.933   1.00 11.37 ?  95  VAL   B O    1 
ATOM   5343 C  CB   . VAL   B 1 95  ? 40.577 -18.908 0.831   1.00 11.00 ?  95  VAL   B CB   1 
ATOM   5344 C  CG1  . VAL   B 1 95  ? 39.196 -19.360 1.316   1.00 12.30 ?  95  VAL   B CG1  1 
ATOM   5345 C  CG2  . VAL   B 1 95  ? 40.447 -17.928 -0.311  1.00 10.91 ?  95  VAL   B CG2  1 
ATOM   5346 H  H    . VAL   B 1 95  ? 43.189 -18.501 1.205   1.00 12.59 ?  95  VAL   B H    1 
ATOM   5347 H  HA   . VAL   B 1 95  ? 40.903 -17.550 2.353   1.00 12.76 ?  95  VAL   B HA   1 
ATOM   5348 H  HB   . VAL   B 1 95  ? 41.038 -19.686 0.494   1.00 13.18 ?  95  VAL   B HB   1 
ATOM   5349 H  HG11 . VAL   B 1 95  ? 38.633 -19.553 0.544   1.00 14.75 ?  95  VAL   B HG11 1 
ATOM   5350 H  HG12 . VAL   B 1 95  ? 39.289 -20.160 1.856   1.00 14.75 ?  95  VAL   B HG12 1 
ATOM   5351 H  HG13 . VAL   B 1 95  ? 38.789 -18.651 1.841   1.00 14.75 ?  95  VAL   B HG13 1 
ATOM   5352 H  HG21 . VAL   B 1 95  ? 39.878 -18.317 -0.994  1.00 13.08 ?  95  VAL   B HG21 1 
ATOM   5353 H  HG22 . VAL   B 1 95  ? 40.048 -17.108 0.023   1.00 13.08 ?  95  VAL   B HG22 1 
ATOM   5354 H  HG23 . VAL   B 1 95  ? 41.326 -17.749 -0.670  1.00 13.08 ?  95  VAL   B HG23 1 
ATOM   5355 N  N    . VAL   B 1 96  ? 40.825 -19.175 4.179   1.00 11.32 ?  96  VAL   B N    1 
ATOM   5356 C  CA   . VAL   B 1 96  ? 40.913 -20.083 5.322   1.00 11.80 ?  96  VAL   B CA   1 
ATOM   5357 C  C    . VAL   B 1 96  ? 39.726 -21.043 5.280   1.00 12.44 ?  96  VAL   B C    1 
ATOM   5358 O  O    . VAL   B 1 96  ? 38.610 -20.690 5.667   1.00 13.28 ?  96  VAL   B O    1 
ATOM   5359 C  CB   . VAL   B 1 96  ? 40.968 -19.330 6.654   1.00 12.52 ?  96  VAL   B CB   1 
ATOM   5360 C  CG1  . VAL   B 1 96  ? 41.131 -20.323 7.801   1.00 13.19 ?  96  VAL   B CG1  1 
ATOM   5361 C  CG2  . VAL   B 1 96  ? 42.086 -18.292 6.662   1.00 13.13 ?  96  VAL   B CG2  1 
ATOM   5362 H  H    . VAL   B 1 96  ? 40.257 -18.541 4.291   1.00 13.57 ?  96  VAL   B H    1 
ATOM   5363 H  HA   . VAL   B 1 96  ? 41.724 -20.612 5.248   1.00 14.14 ?  96  VAL   B HA   1 
ATOM   5364 H  HB   . VAL   B 1 96  ? 40.127 -18.866 6.787   1.00 15.00 ?  96  VAL   B HB   1 
ATOM   5365 H  HG11 . VAL   B 1 96  ? 41.333 -19.835 8.617   1.00 15.81 ?  96  VAL   B HG11 1 
ATOM   5366 H  HG12 . VAL   B 1 96  ? 40.307 -20.823 7.915   1.00 15.81 ?  96  VAL   B HG12 1 
ATOM   5367 H  HG13 . VAL   B 1 96  ? 41.861 -20.930 7.595   1.00 15.81 ?  96  VAL   B HG13 1 
ATOM   5368 H  HG21 . VAL   B 1 96  ? 42.126 -17.873 7.539   1.00 15.73 ?  96  VAL   B HG21 1 
ATOM   5369 H  HG22 . VAL   B 1 96  ? 42.928 -18.726 6.465   1.00 15.73 ?  96  VAL   B HG22 1 
ATOM   5370 H  HG23 . VAL   B 1 96  ? 41.896 -17.616 5.989   1.00 15.73 ?  96  VAL   B HG23 1 
ATOM   5371 N  N    . GLY   B 1 97  ? 39.958 -22.274 4.830   1.00 12.11 ?  97  GLY   B N    1 
ATOM   5372 C  CA   . GLY   B 1 97  ? 38.983 -23.328 4.988   1.00 13.11 ?  97  GLY   B CA   1 
ATOM   5373 C  C    . GLY   B 1 97  ? 39.106 -23.943 6.364   1.00 14.28 ?  97  GLY   B C    1 
ATOM   5374 O  O    . GLY   B 1 97  ? 40.147 -23.819 7.027   1.00 14.82 ?  97  GLY   B O    1 
ATOM   5375 H  H    . GLY   B 1 97  ? 40.683 -22.517 4.427   1.00 14.51 ?  97  GLY   B H    1 
ATOM   5376 H  HA2  . GLY   B 1 97  ? 38.089 -22.958 4.870   1.00 15.72 ?  97  GLY   B HA2  1 
ATOM   5377 H  HA3  . GLY   B 1 97  ? 39.123 -24.011 4.311   1.00 15.72 ?  97  GLY   B HA3  1 
ATOM   5378 N  N    . PRO   B 1 98  ? 38.061 -24.634 6.819   1.00 15.39 ?  98  PRO   B N    1 
ATOM   5379 C  CA   . PRO   B 1 98  ? 38.154 -25.331 8.105   1.00 16.35 ?  98  PRO   B CA   1 
ATOM   5380 C  C    . PRO   B 1 98  ? 39.186 -26.448 8.063   1.00 16.05 ?  98  PRO   B C    1 
ATOM   5381 O  O    . PRO   B 1 98  ? 39.297 -27.184 7.083   1.00 16.17 ?  98  PRO   B O    1 
ATOM   5382 C  CB   . PRO   B 1 98  ? 36.736 -25.879 8.314   1.00 16.50 ?  98  PRO   B CB   1 
ATOM   5383 C  CG   . PRO   B 1 98  ? 36.165 -25.994 6.946   1.00 16.14 ?  98  PRO   B CG   1 
ATOM   5384 C  CD   . PRO   B 1 98  ? 36.738 -24.818 6.192   1.00 15.49 ?  98  PRO   B CD   1 
ATOM   5385 H  HA   . PRO   B 1 98  ? 38.373 -24.711 8.811   1.00 19.61 ?  98  PRO   B HA   1 
ATOM   5386 H  HB2  . PRO   B 1 98  ? 36.784 -26.751 8.741   1.00 19.79 ?  98  PRO   B HB2  1 
ATOM   5387 H  HB3  . PRO   B 1 98  ? 36.223 -25.260 8.850   1.00 19.79 ?  98  PRO   B HB3  1 
ATOM   5388 H  HG2  . PRO   B 1 98  ? 36.447 -26.833 6.542   1.00 19.35 ?  98  PRO   B HG2  1 
ATOM   5389 H  HG3  . PRO   B 1 98  ? 35.199 -25.943 6.990   1.00 19.35 ?  98  PRO   B HG3  1 
ATOM   5390 H  HD2  . PRO   B 1 98  ? 36.826 -25.033 5.247   1.00 18.58 ?  98  PRO   B HD2  1 
ATOM   5391 H  HD3  . PRO   B 1 98  ? 36.187 -24.031 6.325   1.00 18.58 ?  98  PRO   B HD3  1 
ATOM   5392 N  N    . ASN   B 1 99  ? 39.947 -26.566 9.146   1.00 17.31 ?  99  ASN   B N    1 
ATOM   5393 C  CA   . ASN   B 1 99  ? 40.931 -27.635 9.316   1.00 18.35 ?  99  ASN   B CA   1 
ATOM   5394 C  C    . ASN   B 1 99  ? 40.310 -28.716 10.198  1.00 21.49 ?  99  ASN   B C    1 
ATOM   5395 O  O    . ASN   B 1 99  ? 40.248 -28.575 11.422  1.00 22.11 ?  99  ASN   B O    1 
ATOM   5396 C  CB   . ASN   B 1 99  ? 42.202 -27.074 9.940   1.00 18.44 ?  99  ASN   B CB   1 
ATOM   5397 C  CG   . ASN   B 1 99  ? 43.337 -28.074 9.951   1.00 19.18 ?  99  ASN   B CG   1 
ATOM   5398 O  OD1  . ASN   B 1 99  ? 43.120 -29.266 10.137  1.00 20.18 ?  99  ASN   B OD1  1 
ATOM   5399 N  ND2  . ASN   B 1 99  ? 44.552 -27.595 9.742   1.00 18.85 ?  99  ASN   B ND2  1 
ATOM   5400 H  H    . ASN   B 1 99  ? 39.907 -26.025 9.810   1.00 20.75 ?  99  ASN   B H    1 
ATOM   5401 H  HA   . ASN   B 1 99  ? 41.143 -28.027 8.454   1.00 22.01 ?  99  ASN   B HA   1 
ATOM   5402 H  HB2  . ASN   B 1 99  ? 42.481 -26.300 9.434   1.00 22.11 ?  99  ASN   B HB2  1 
ATOM   5403 H  HB3  . ASN   B 1 99  ? 42.011 -26.826 10.859  1.00 22.11 ?  99  ASN   B HB3  1 
ATOM   5404 H  HD21 . ASN   B 1 99  ? 45.227 -28.124 9.734   1.00 22.61 ?  99  ASN   B HD21 1 
ATOM   5405 H  HD22 . ASN   B 1 99  ? 44.659 -26.752 9.617   1.00 22.61 ?  99  ASN   B HD22 1 
ATOM   5406 N  N    A VAL   B 1 100 ? 39.834 -29.795 9.570   0.70 23.52 ?  100 VAL   B N    1 
ATOM   5407 N  N    B VAL   B 1 100 ? 39.849 -29.799 9.565   0.30 23.65 ?  100 VAL   B N    1 
ATOM   5408 C  CA   A VAL   B 1 100 ? 39.218 -30.883 10.328  0.70 26.21 ?  100 VAL   B CA   1 
ATOM   5409 C  CA   B VAL   B 1 100 ? 39.224 -30.894 10.302  0.30 25.88 ?  100 VAL   B CA   1 
ATOM   5410 C  C    A VAL   B 1 100 ? 40.228 -31.552 11.253  0.70 26.87 ?  100 VAL   B C    1 
ATOM   5411 C  C    B VAL   B 1 100 ? 40.223 -31.564 11.236  0.30 26.69 ?  100 VAL   B C    1 
ATOM   5412 O  O    A VAL   B 1 100 ? 39.862 -32.055 12.322  0.70 27.44 ?  100 VAL   B O    1 
ATOM   5413 O  O    B VAL   B 1 100 ? 39.847 -32.071 12.300  0.30 26.92 ?  100 VAL   B O    1 
ATOM   5414 C  CB   A VAL   B 1 100 ? 38.547 -31.893 9.375   0.70 28.43 ?  100 VAL   B CB   1 
ATOM   5415 C  CB   B VAL   B 1 100 ? 38.581 -31.894 9.319   0.30 27.30 ?  100 VAL   B CB   1 
ATOM   5416 C  CG1  A VAL   B 1 100 ? 38.056 -33.111 10.143  0.70 29.51 ?  100 VAL   B CG1  1 
ATOM   5417 C  CG1  B VAL   B 1 100 ? 38.079 -33.126 10.055  0.30 27.89 ?  100 VAL   B CG1  1 
ATOM   5418 C  CG2  A VAL   B 1 100 ? 37.395 -31.233 8.637   0.70 29.03 ?  100 VAL   B CG2  1 
ATOM   5419 C  CG2  B VAL   B 1 100 ? 37.444 -31.226 8.560   0.30 27.78 ?  100 VAL   B CG2  1 
ATOM   5420 H  H    A VAL   B 1 100 ? 39.840 -29.908 8.715   0.70 28.20 ?  100 VAL   B H    1 
ATOM   5421 H  H    B VAL   B 1 100 ? 39.882 -29.917 8.713   0.30 28.36 ?  100 VAL   B H    1 
ATOM   5422 H  HA   A VAL   B 1 100 ? 38.513 -30.507 10.881  0.70 31.43 ?  100 VAL   B HA   1 
ATOM   5423 H  HA   B VAL   B 1 100 ? 38.511 -30.529 10.847  0.30 31.04 ?  100 VAL   B HA   1 
ATOM   5424 H  HB   A VAL   B 1 100 ? 39.196 -32.194 8.721   0.70 34.11 ?  100 VAL   B HB   1 
ATOM   5425 H  HB   B VAL   B 1 100 ? 39.246 -32.180 8.674   0.30 32.75 ?  100 VAL   B HB   1 
ATOM   5426 H  HG11 A VAL   B 1 100 ? 37.455 -33.621 9.576   0.70 35.40 ?  100 VAL   B HG11 1 
ATOM   5427 H  HG11 B VAL   B 1 100 ? 37.493 -33.627 9.464   0.30 33.45 ?  100 VAL   B HG11 1 
ATOM   5428 H  HG12 A VAL   B 1 100 ? 38.815 -33.661 10.393  0.70 35.40 ?  100 VAL   B HG12 1 
ATOM   5429 H  HG12 B VAL   B 1 100 ? 38.836 -33.676 10.310  0.30 33.45 ?  100 VAL   B HG12 1 
ATOM   5430 H  HG13 A VAL   B 1 100 ? 37.584 -32.816 10.938  0.70 35.40 ?  100 VAL   B HG13 1 
ATOM   5431 H  HG13 B VAL   B 1 100 ? 37.589 -32.846 10.843  0.30 33.45 ?  100 VAL   B HG13 1 
ATOM   5432 H  HG21 A VAL   B 1 100 ? 36.976 -31.887 8.055   0.70 34.82 ?  100 VAL   B HG21 1 
ATOM   5433 H  HG21 B VAL   B 1 100 ? 37.037 -31.875 7.965   0.30 33.31 ?  100 VAL   B HG21 1 
ATOM   5434 H  HG22 A VAL   B 1 100 ? 36.750 -30.908 9.286   0.70 34.82 ?  100 VAL   B HG22 1 
ATOM   5435 H  HG22 B VAL   B 1 100 ? 36.786 -30.904 9.198   0.30 33.31 ?  100 VAL   B HG22 1 
ATOM   5436 H  HG23 A VAL   B 1 100 ? 37.738 -30.495 8.113   0.70 34.82 ?  100 VAL   B HG23 1 
ATOM   5437 H  HG23 B VAL   B 1 100 ? 37.799 -30.483 8.049   0.30 33.31 ?  100 VAL   B HG23 1 
ATOM   5438 N  N    . ASN   B 1 101 ? 41.503 -31.591 10.858  1.00 27.26 ?  101 ASN   B N    1 
ATOM   5439 C  CA   . ASN   B 1 101 ? 42.541 -32.129 11.736  1.00 28.81 ?  101 ASN   B CA   1 
ATOM   5440 C  C    . ASN   B 1 101 ? 42.742 -31.289 12.992  1.00 31.02 ?  101 ASN   B C    1 
ATOM   5441 O  O    . ASN   B 1 101 ? 43.389 -31.762 13.935  1.00 32.12 ?  101 ASN   B O    1 
ATOM   5442 C  CB   . ASN   B 1 101 ? 43.865 -32.267 10.981  1.00 28.66 ?  101 ASN   B CB   1 
ATOM   5443 C  CG   . ASN   B 1 101 ? 43.858 -33.426 10.002  1.00 28.33 ?  101 ASN   B CG   1 
ATOM   5444 O  OD1  . ASN   B 1 101 ? 43.198 -34.434 10.228  1.00 28.77 ?  101 ASN   B OD1  1 
ATOM   5445 N  ND2  . ASN   B 1 101 ? 44.589 -33.282 8.906   1.00 27.96 ?  101 ASN   B ND2  1 
ATOM   5446 H  H    A ASN   B 1 101 ? 41.784 -31.334 10.087  0.70 32.70 ?  101 ASN   B H    1 
ATOM   5447 H  H    B ASN   B 1 101 ? 41.790 -31.315 10.096  0.30 32.70 ?  101 ASN   B H    1 
ATOM   5448 H  HA   . ASN   B 1 101 ? 42.272 -33.011 12.023  1.00 34.56 ?  101 ASN   B HA   1 
ATOM   5449 H  HB2  . ASN   B 1 101 ? 44.038 -31.457 10.480  1.00 34.38 ?  101 ASN   B HB2  1 
ATOM   5450 H  HB3  . ASN   B 1 101 ? 44.579 -32.419 11.623  1.00 34.38 ?  101 ASN   B HB3  1 
ATOM   5451 H  HD21 . ASN   B 1 101 ? 44.615 -33.914 8.324   1.00 33.53 ?  101 ASN   B HD21 1 
ATOM   5452 H  HD22 . ASN   B 1 101 ? 45.031 -32.558 8.777   1.00 33.53 ?  101 ASN   B HD22 1 
ATOM   5453 N  N    . LYS   B 1 102 ? 42.218 -30.062 13.019  1.00 33.52 ?  102 LYS   B N    1 
ATOM   5454 C  CA   . LYS   B 1 102 ? 42.183 -29.232 14.215  1.00 36.40 ?  102 LYS   B CA   1 
ATOM   5455 C  C    . LYS   B 1 102 ? 40.796 -29.185 14.845  1.00 35.84 ?  102 LYS   B C    1 
ATOM   5456 O  O    . LYS   B 1 102 ? 40.566 -28.383 15.755  1.00 36.38 ?  102 LYS   B O    1 
ATOM   5457 C  CB   . LYS   B 1 102 ? 42.635 -27.806 13.892  1.00 39.88 ?  102 LYS   B CB   1 
ATOM   5458 C  CG   . LYS   B 1 102 ? 44.100 -27.660 13.517  1.00 42.89 ?  102 LYS   B CG   1 
ATOM   5459 C  CD   . LYS   B 1 102 ? 44.381 -26.235 13.064  1.00 45.77 ?  102 LYS   B CD   1 
ATOM   5460 C  CE   . LYS   B 1 102 ? 45.860 -25.983 12.833  1.00 47.80 ?  102 LYS   B CE   1 
ATOM   5461 N  NZ   . LYS   B 1 102 ? 46.098 -24.585 12.369  1.00 49.03 ?  102 LYS   B NZ   1 
ATOM   5462 H  H    . LYS   B 1 102 ? 41.865 -29.679 12.334  1.00 40.20 ?  102 LYS   B H    1 
ATOM   5463 H  HA   . LYS   B 1 102 ? 42.797 -29.595 14.870  1.00 43.66 ?  102 LYS   B HA   1 
ATOM   5464 H  HB2  . LYS   B 1 102 ? 42.111 -27.474 13.147  1.00 47.84 ?  102 LYS   B HB2  1 
ATOM   5465 H  HB3  . LYS   B 1 102 ? 42.480 -27.247 14.672  1.00 47.84 ?  102 LYS   B HB3  1 
ATOM   5466 H  HG2  . LYS   B 1 102 ? 44.655 -27.853 14.290  1.00 51.45 ?  102 LYS   B HG2  1 
ATOM   5467 H  HG3  . LYS   B 1 102 ? 44.311 -28.264 12.788  1.00 51.45 ?  102 LYS   B HG3  1 
ATOM   5468 H  HD2  . LYS   B 1 102 ? 43.913 -26.070 12.230  1.00 54.91 ?  102 LYS   B HD2  1 
ATOM   5469 H  HD3  . LYS   B 1 102 ? 44.073 -25.618 13.746  1.00 54.91 ?  102 LYS   B HD3  1 
ATOM   5470 H  HE2  . LYS   B 1 102 ? 46.343 -26.116 13.664  1.00 57.34 ?  102 LYS   B HE2  1 
ATOM   5471 H  HE3  . LYS   B 1 102 ? 46.187 -26.591 12.152  1.00 57.34 ?  102 LYS   B HE3  1 
ATOM   5472 H  HZ1  . LYS   B 1 102 ? 46.968 -24.452 12.238  1.00 58.82 ?  102 LYS   B HZ1  1 
ATOM   5473 H  HZ2  . LYS   B 1 102 ? 45.665 -24.440 11.605  1.00 58.82 ?  102 LYS   B HZ2  1 
ATOM   5474 H  HZ3  . LYS   B 1 102 ? 45.806 -24.008 12.981  1.00 58.82 ?  102 LYS   B HZ3  1 
ATOM   5475 N  N    . GLY   B 1 103 ? 39.865 -30.010 14.372  1.00 35.26 ?  103 GLY   B N    1 
ATOM   5476 C  CA   . GLY   B 1 103 ? 38.534 -30.067 14.941  1.00 34.69 ?  103 GLY   B CA   1 
ATOM   5477 C  C    . GLY   B 1 103 ? 37.588 -28.980 14.488  1.00 33.60 ?  103 GLY   B C    1 
ATOM   5478 O  O    . GLY   B 1 103 ? 36.498 -28.856 15.058  1.00 33.99 ?  103 GLY   B O    1 
ATOM   5479 H  H    . GLY   B 1 103 ? 39.984 -30.549 13.714  1.00 42.29 ?  103 GLY   B H    1 
ATOM   5480 H  HA2  . GLY   B 1 103 ? 38.134 -30.921 14.719  1.00 41.62 ?  103 GLY   B HA2  1 
ATOM   5481 H  HA3  . GLY   B 1 103 ? 38.603 -30.013 15.908  1.00 41.62 ?  103 GLY   B HA3  1 
ATOM   5482 N  N    A GLU   B 1 104 ? 37.971 -28.180 13.495  0.70 32.51 ?  104 GLU   B N    1 
ATOM   5483 N  N    B GLU   B 1 104 ? 37.952 -28.200 13.475  0.30 32.88 ?  104 GLU   B N    1 
ATOM   5484 C  CA   A GLU   B 1 104 ? 37.131 -27.080 13.048  0.70 31.34 ?  104 GLU   B CA   1 
ATOM   5485 C  CA   B GLU   B 1 104 ? 37.096 -27.116 13.019  0.30 32.01 ?  104 GLU   B CA   1 
ATOM   5486 C  C    A GLU   B 1 104 ? 35.942 -27.603 12.241  0.70 31.59 ?  104 GLU   B C    1 
ATOM   5487 C  C    B GLU   B 1 104 ? 35.934 -27.656 12.190  0.30 32.07 ?  104 GLU   B C    1 
ATOM   5488 O  O    A GLU   B 1 104 ? 35.976 -28.691 11.657  0.70 32.09 ?  104 GLU   B O    1 
ATOM   5489 O  O    B GLU   B 1 104 ? 36.014 -28.729 11.586  0.30 32.25 ?  104 GLU   B O    1 
ATOM   5490 C  CB   A GLU   B 1 104 ? 37.961 -26.080 12.240  0.70 30.28 ?  104 GLU   B CB   1 
ATOM   5491 C  CB   B GLU   B 1 104 ? 37.913 -26.100 12.222  0.30 31.14 ?  104 GLU   B CB   1 
ATOM   5492 C  CG   A GLU   B 1 104 ? 39.063 -25.432 13.072  0.70 29.13 ?  104 GLU   B CG   1 
ATOM   5493 C  CG   B GLU   B 1 104 ? 39.014 -25.455 13.055  0.30 30.35 ?  104 GLU   B CG   1 
ATOM   5494 C  CD   A GLU   B 1 104 ? 39.996 -24.549 12.269  0.70 27.84 ?  104 GLU   B CD   1 
ATOM   5495 C  CD   B GLU   B 1 104 ? 39.949 -24.585 12.240  0.30 29.64 ?  104 GLU   B CD   1 
ATOM   5496 O  OE1  A GLU   B 1 104 ? 39.979 -24.612 11.022  0.70 26.11 ?  104 GLU   B OE1  1 
ATOM   5497 O  OE1  B GLU   B 1 104 ? 39.873 -24.619 10.994  0.30 29.03 ?  104 GLU   B OE1  1 
ATOM   5498 O  OE2  A GLU   B 1 104 ? 40.756 -23.787 12.901  0.70 27.60 -1 104 GLU   B OE2  1 
ATOM   5499 O  OE2  B GLU   B 1 104 ? 40.765 -23.865 12.852  0.30 29.44 -1 104 GLU   B OE2  1 
ATOM   5500 H  H    A GLU   B 1 104 ? 38.716 -28.250 13.072  0.70 39.00 ?  104 GLU   B H    1 
ATOM   5501 H  H    B GLU   B 1 104 ? 38.691 -28.275 13.038  0.30 39.45 ?  104 GLU   B H    1 
ATOM   5502 H  HA   A GLU   B 1 104 ? 36.787 -26.613 13.826  0.70 37.59 ?  104 GLU   B HA   1 
ATOM   5503 H  HA   B GLU   B 1 104 ? 36.727 -26.663 13.791  0.30 38.39 ?  104 GLU   B HA   1 
ATOM   5504 H  HB2  A GLU   B 1 104 ? 38.378 -26.540 11.495  0.70 36.32 ?  104 GLU   B HB2  1 
ATOM   5505 H  HB2  B GLU   B 1 104 ? 38.329 -26.546 11.468  0.30 37.35 ?  104 GLU   B HB2  1 
ATOM   5506 H  HB3  A GLU   B 1 104 ? 37.379 -25.376 11.912  0.70 36.32 ?  104 GLU   B HB3  1 
ATOM   5507 H  HB3  B GLU   B 1 104 ? 37.324 -25.396 11.908  0.30 37.35 ?  104 GLU   B HB3  1 
ATOM   5508 H  HG2  A GLU   B 1 104 ? 38.658 -24.879 13.759  0.70 34.94 ?  104 GLU   B HG2  1 
ATOM   5509 H  HG2  B GLU   B 1 104 ? 38.607 -24.897 13.737  0.30 36.41 ?  104 GLU   B HG2  1 
ATOM   5510 H  HG3  A GLU   B 1 104 ? 39.601 -26.125 13.482  0.70 34.94 ?  104 GLU   B HG3  1 
ATOM   5511 H  HG3  B GLU   B 1 104 ? 39.542 -26.153 13.475  0.30 36.41 ?  104 GLU   B HG3  1 
ATOM   5512 N  N    A ASP   B 1 105 ? 34.876 -26.805 12.221  0.70 31.04 ?  105 ASP   B N    1 
ATOM   5513 N  N    B ASP   B 1 105 ? 34.842 -26.892 12.172  0.30 31.69 ?  105 ASP   B N    1 
ATOM   5514 C  CA   A ASP   B 1 105 ? 33.599 -27.250 11.674  0.70 31.48 ?  105 ASP   B CA   1 
ATOM   5515 C  CA   B ASP   B 1 105 ? 33.586 -27.365 11.601  0.30 31.68 ?  105 ASP   B CA   1 
ATOM   5516 C  C    A ASP   B 1 105 ? 33.659 -27.302 10.151  0.70 29.43 ?  105 ASP   B C    1 
ATOM   5517 C  C    B ASP   B 1 105 ? 33.669 -27.379 10.078  0.30 30.61 ?  105 ASP   B C    1 
ATOM   5518 O  O    A ASP   B 1 105 ? 33.827 -26.272 9.492   0.70 28.47 ?  105 ASP   B O    1 
ATOM   5519 O  O    B ASP   B 1 105 ? 33.881 -26.337 9.448   0.30 30.28 ?  105 ASP   B O    1 
ATOM   5520 C  CB   A ASP   B 1 105 ? 32.489 -26.304 12.126  0.70 34.14 ?  105 ASP   B CB   1 
ATOM   5521 C  CB   B ASP   B 1 105 ? 32.440 -26.467 12.064  0.30 32.64 ?  105 ASP   B CB   1 
ATOM   5522 C  CG   A ASP   B 1 105 ? 31.111 -26.781 11.708  0.70 36.74 ?  105 ASP   B CG   1 
ATOM   5523 C  CG   B ASP   B 1 105 ? 31.077 -27.032 11.706  0.30 33.63 ?  105 ASP   B CG   1 
ATOM   5524 O  OD1  A ASP   B 1 105 ? 31.009 -27.884 11.129  0.70 37.02 ?  105 ASP   B OD1  1 
ATOM   5525 O  OD1  B ASP   B 1 105 ? 31.024 -28.079 11.027  0.30 33.83 ?  105 ASP   B OD1  1 
ATOM   5526 O  OD2  A ASP   B 1 105 ? 30.126 -26.052 11.958  0.70 38.07 -1 105 ASP   B OD2  1 
ATOM   5527 O  OD2  B ASP   B 1 105 ? 30.057 -26.434 12.111  0.30 33.97 -1 105 ASP   B OD2  1 
ATOM   5528 H  H    A ASP   B 1 105 ? 34.869 -26.001 12.523  0.70 37.23 ?  105 ASP   B H    1 
ATOM   5529 H  H    B ASP   B 1 105 ? 34.807 -26.093 12.482  0.30 38.02 ?  105 ASP   B H    1 
ATOM   5530 H  HA   A ASP   B 1 105 ? 33.399 -28.139 12.005  0.70 37.76 ?  105 ASP   B HA   1 
ATOM   5531 H  HA   B ASP   B 1 105 ? 33.405 -28.268 11.906  0.30 38.00 ?  105 ASP   B HA   1 
ATOM   5532 H  HB2  A ASP   B 1 105 ? 32.511 -26.226 13.094  0.70 40.96 ?  105 ASP   B HB2  1 
ATOM   5533 H  HB2  B ASP   B 1 105 ? 32.480 -26.372 13.030  0.30 39.15 ?  105 ASP   B HB2  1 
ATOM   5534 H  HB3  A ASP   B 1 105 ? 32.629 -25.433 11.721  0.70 40.96 ?  105 ASP   B HB3  1 
ATOM   5535 H  HB3  B ASP   B 1 105 ? 32.529 -25.595 11.644  0.30 39.15 ?  105 ASP   B HB3  1 
ATOM   5536 N  N    A ILE   B 1 106 ? 33.485 -28.504 9.596   0.70 28.55 ?  106 ILE   B N    1 
ATOM   5537 N  N    B ILE   B 1 106 ? 33.490 -28.565 9.490   0.30 29.70 ?  106 ILE   B N    1 
ATOM   5538 C  CA   A ILE   B 1 106 ? 33.490 -28.690 8.150   0.70 27.43 ?  106 ILE   B CA   1 
ATOM   5539 C  CA   B ILE   B 1 106 ? 33.504 -28.712 8.039   0.30 28.92 ?  106 ILE   B CA   1 
ATOM   5540 C  C    A ILE   B 1 106 ? 32.397 -27.873 7.469   0.70 26.07 ?  106 ILE   B C    1 
ATOM   5541 C  C    B ILE   B 1 106 ? 32.402 -27.896 7.375   0.30 28.03 ?  106 ILE   B C    1 
ATOM   5542 O  O    A ILE   B 1 106 ? 32.504 -27.568 6.277   0.70 25.15 ?  106 ILE   B O    1 
ATOM   5543 O  O    B ILE   B 1 106 ? 32.478 -27.616 6.174   0.30 27.76 ?  106 ILE   B O    1 
ATOM   5544 C  CB   A ILE   B 1 106 ? 33.387 -30.196 7.819   0.70 28.24 ?  106 ILE   B CB   1 
ATOM   5545 C  CB   B ILE   B 1 106 ? 33.417 -30.211 7.669   0.30 29.15 ?  106 ILE   B CB   1 
ATOM   5546 C  CG1  A ILE   B 1 106 ? 33.653 -30.453 6.335   0.70 28.66 ?  106 ILE   B CG1  1 
ATOM   5547 C  CG1  B ILE   B 1 106 ? 33.688 -30.429 6.178   0.30 29.18 ?  106 ILE   B CG1  1 
ATOM   5548 C  CG2  A ILE   B 1 106 ? 32.019 -30.741 8.218   0.70 28.71 ?  106 ILE   B CG2  1 
ATOM   5549 C  CG2  B ILE   B 1 106 ? 32.058 -30.783 8.053   0.30 29.43 ?  106 ILE   B CG2  1 
ATOM   5550 C  CD1  A ILE   B 1 106 ? 35.021 -30.003 5.881   0.70 28.71 ?  106 ILE   B CD1  1 
ATOM   5551 C  CD1  B ILE   B 1 106 ? 35.044 -29.937 5.728   0.30 29.20 ?  106 ILE   B CD1  1 
ATOM   5552 H  H    A ILE   B 1 106 ? 33.358 -29.226 10.042  0.70 34.25 ?  106 ILE   B H    1 
ATOM   5553 H  H    B ILE   B 1 106 ? 33.368 -29.300 9.914   0.30 35.62 ?  106 ILE   B H    1 
ATOM   5554 H  HA   A ILE   B 1 106 ? 34.337 -28.372 7.811   0.70 32.90 ?  106 ILE   B HA   1 
ATOM   5555 H  HA   B ILE   B 1 106 ? 34.349 -28.374 7.711   0.30 34.69 ?  106 ILE   B HA   1 
ATOM   5556 H  HB   A ILE   B 1 106 ? 34.059 -30.668 8.335   0.70 33.87 ?  106 ILE   B HB   1 
ATOM   5557 H  HB   B ILE   B 1 106 ? 34.095 -30.686 8.171   0.30 34.97 ?  106 ILE   B HB   1 
ATOM   5558 H  HG12 A ILE   B 1 106 ? 33.586 -31.407 6.166   0.70 34.37 ?  106 ILE   B HG12 1 
ATOM   5559 H  HG12 B ILE   B 1 106 ? 33.645 -31.382 5.990   0.30 35.00 ?  106 ILE   B HG12 1 
ATOM   5560 H  HG13 A ILE   B 1 106 ? 32.993 -29.980 5.808   0.70 34.37 ?  106 ILE   B HG13 1 
ATOM   5561 H  HG13 B ILE   B 1 106 ? 33.015 -29.963 5.661   0.30 35.00 ?  106 ILE   B HG13 1 
ATOM   5562 H  HG21 A ILE   B 1 106 ? 32.032 -31.708 8.148   0.70 34.43 ?  106 ILE   B HG21 1 
ATOM   5563 H  HG21 B ILE   B 1 106 ? 32.080 -31.747 7.944   0.30 35.30 ?  106 ILE   B HG21 1 
ATOM   5564 H  HG22 A ILE   B 1 106 ? 31.830 -30.480 9.134   0.70 34.43 ?  106 ILE   B HG22 1 
ATOM   5565 H  HG22 B ILE   B 1 106 ? 31.872 -30.560 8.978   0.30 35.30 ?  106 ILE   B HG22 1 
ATOM   5566 H  HG23 A ILE   B 1 106 ? 31.345 -30.375 7.625   0.70 34.43 ?  106 ILE   B HG23 1 
ATOM   5567 H  HG23 B ILE   B 1 106 ? 31.377 -30.401 7.478   0.30 35.30 ?  106 ILE   B HG23 1 
ATOM   5568 H  HD11 A ILE   B 1 106 ? 35.220 -30.415 5.027   0.70 34.44 ?  106 ILE   B HD11 1 
ATOM   5569 H  HD11 B ILE   B 1 106 ? 35.247 -30.323 4.863   0.30 35.02 ?  106 ILE   B HD11 1 
ATOM   5570 H  HD12 A ILE   B 1 106 ? 35.022 -29.037 5.789   0.70 34.44 ?  106 ILE   B HD12 1 
ATOM   5571 H  HD12 B ILE   B 1 106 ? 35.021 -28.969 5.661   0.30 35.02 ?  106 ILE   B HD12 1 
ATOM   5572 H  HD13 A ILE   B 1 106 ? 35.679 -30.275 6.541   0.70 34.44 ?  106 ILE   B HD13 1 
ATOM   5573 H  HD13 B ILE   B 1 106 ? 35.710 -30.210 6.378   0.30 35.02 ?  106 ILE   B HD13 1 
ATOM   5574 N  N    A GLN   B 1 107 ? 31.346 -27.498 8.203   0.70 26.22 ?  107 GLN   B N    1 
ATOM   5575 N  N    B GLN   B 1 107 ? 31.373 -27.503 8.130   0.30 27.71 ?  107 GLN   B N    1 
ATOM   5576 C  CA   A GLN   B 1 107 ? 30.271 -26.703 7.618   0.70 26.50 ?  107 GLN   B CA   1 
ATOM   5577 C  CA   B GLN   B 1 107 ? 30.286 -26.711 7.564   0.30 27.35 ?  107 GLN   B CA   1 
ATOM   5578 C  C    A GLN   B 1 107 ? 30.757 -25.354 7.104   0.70 24.32 ?  107 GLN   B C    1 
ATOM   5579 C  C    B GLN   B 1 107 ? 30.756 -25.340 7.096   0.30 24.91 ?  107 GLN   B C    1 
ATOM   5580 O  O    A GLN   B 1 107 ? 30.111 -24.773 6.227   0.70 24.72 ?  107 GLN   B O    1 
ATOM   5581 O  O    B GLN   B 1 107 ? 30.094 -24.727 6.252   0.30 25.09 ?  107 GLN   B O    1 
ATOM   5582 C  CB   A GLN   B 1 107 ? 29.155 -26.498 8.648   0.70 30.10 ?  107 GLN   B CB   1 
ATOM   5583 C  CB   B GLN   B 1 107 ? 29.164 -26.565 8.596   0.30 29.72 ?  107 GLN   B CB   1 
ATOM   5584 C  CG   A GLN   B 1 107 ? 27.833 -25.997 8.068   0.70 33.61 ?  107 GLN   B CG   1 
ATOM   5585 C  CG   B GLN   B 1 107 ? 27.838 -26.061 8.036   0.30 31.87 ?  107 GLN   B CG   1 
ATOM   5586 C  CD   A GLN   B 1 107 ? 27.759 -24.483 7.968   0.70 36.37 ?  107 GLN   B CD   1 
ATOM   5587 C  CD   B GLN   B 1 107 ? 27.729 -24.547 8.047   0.30 33.59 ?  107 GLN   B CD   1 
ATOM   5588 O  OE1  A GLN   B 1 107 ? 28.596 -23.769 8.524   0.70 37.40 ?  107 GLN   B OE1  1 
ATOM   5589 O  OE1  B GLN   B 1 107 ? 28.556 -23.855 8.642   0.30 34.17 ?  107 GLN   B OE1  1 
ATOM   5590 N  NE2  A GLN   B 1 107 ? 26.749 -23.985 7.259   0.70 37.25 ?  107 GLN   B NE2  1 
ATOM   5591 N  NE2  B GLN   B 1 107 ? 26.699 -24.025 7.388   0.30 34.20 ?  107 GLN   B NE2  1 
ATOM   5592 H  H    A GLN   B 1 107 ? 31.236 -27.687 9.030   0.70 31.45 ?  107 GLN   B H    1 
ATOM   5593 H  H    B GLN   B 1 107 ? 31.281 -27.681 8.964   0.30 33.23 ?  107 GLN   B H    1 
ATOM   5594 H  HA   A GLN   B 1 107 ? 29.894 -27.189 6.868   0.70 31.78 ?  107 GLN   B HA   1 
ATOM   5595 H  HA   B GLN   B 1 107 ? 29.922 -27.180 6.798   0.30 32.81 ?  107 GLN   B HA   1 
ATOM   5596 H  HB2  A GLN   B 1 107 ? 28.981 -27.344 9.082   0.70 36.10 ?  107 GLN   B HB2  1 
ATOM   5597 H  HB2  B GLN   B 1 107 ? 28.999 -27.432 8.992   0.30 35.64 ?  107 GLN   B HB2  1 
ATOM   5598 H  HB3  A GLN   B 1 107 ? 29.455 -25.849 9.304   0.70 36.10 ?  107 GLN   B HB3  1 
ATOM   5599 H  HB3  B GLN   B 1 107 ? 29.451 -25.943 9.282   0.30 35.64 ?  107 GLN   B HB3  1 
ATOM   5600 H  HG2  A GLN   B 1 107 ? 27.719 -26.358 7.176   0.70 40.31 ?  107 GLN   B HG2  1 
ATOM   5601 H  HG2  B GLN   B 1 107 ? 27.745 -26.360 7.119   0.30 38.23 ?  107 GLN   B HG2  1 
ATOM   5602 H  HG3  A GLN   B 1 107 ? 27.105 -26.297 8.640   0.70 40.31 ?  107 GLN   B HG3  1 
ATOM   5603 H  HG3  B GLN   B 1 107 ? 27.112 -26.419 8.575   0.30 38.23 ?  107 GLN   B HG3  1 
ATOM   5604 H  HE21 A GLN   B 1 107 ? 26.183 -24.514 6.883   0.70 44.68 ?  107 GLN   B HE21 1 
ATOM   5605 H  HE21 B GLN   B 1 107 ? 26.141 -24.539 6.983   0.30 41.02 ?  107 GLN   B HE21 1 
ATOM   5606 H  HE22 A GLN   B 1 107 ? 26.658 -23.133 7.174   0.70 44.68 ?  107 GLN   B HE22 1 
ATOM   5607 H  HE22 B GLN   B 1 107 ? 26.591 -23.172 7.367   0.30 41.02 ?  107 GLN   B HE22 1 
ATOM   5608 N  N    . LEU   B 1 108 ? 31.881 -24.846 7.618   1.00 22.60 ?  108 LEU   B N    1 
ATOM   5609 C  CA   . LEU   B 1 108 ? 32.422 -23.550 7.206   1.00 19.70 ?  108 LEU   B CA   1 
ATOM   5610 C  C    . LEU   B 1 108 ? 33.069 -23.578 5.830   1.00 17.08 ?  108 LEU   B C    1 
ATOM   5611 O  O    . LEU   B 1 108 ? 33.504 -22.522 5.342   1.00 16.30 ?  108 LEU   B O    1 
ATOM   5612 C  CB   . LEU   B 1 108 ? 33.423 -23.055 8.247   1.00 20.18 ?  108 LEU   B CB   1 
ATOM   5613 C  CG   . LEU   B 1 108 ? 32.795 -22.553 9.547   1.00 21.48 ?  108 LEU   B CG   1 
ATOM   5614 C  CD1  . LEU   B 1 108 ? 33.807 -22.562 10.674  1.00 21.56 ?  108 LEU   B CD1  1 
ATOM   5615 C  CD2  . LEU   B 1 108 ? 32.244 -21.150 9.347   1.00 22.23 ?  108 LEU   B CD2  1 
ATOM   5616 H  H    A LEU   B 1 108 ? 32.343 -25.235 8.224   0.70 27.10 ?  108 LEU   B H    1 
ATOM   5617 H  H    B LEU   B 1 108 ? 32.341 -25.240 8.223   0.30 27.10 ?  108 LEU   B H    1 
ATOM   5618 H  HA   . LEU   B 1 108 ? 31.694 -22.913 7.171   1.00 23.63 ?  108 LEU   B HA   1 
ATOM   5619 H  HB2  . LEU   B 1 108 ? 34.018 -23.784 8.478   1.00 24.20 ?  108 LEU   B HB2  1 
ATOM   5620 H  HB3  . LEU   B 1 108 ? 33.929 -22.323 7.867   1.00 24.20 ?  108 LEU   B HB3  1 
ATOM   5621 H  HG   . LEU   B 1 108 ? 32.056 -23.133 9.796   1.00 25.76 ?  108 LEU   B HG   1 
ATOM   5622 H  HD11 . LEU   B 1 108 ? 33.376 -22.262 11.490  1.00 25.85 ?  108 LEU   B HD11 1 
ATOM   5623 H  HD12 . LEU   B 1 108 ? 34.142 -23.464 10.789  1.00 25.85 ?  108 LEU   B HD12 1 
ATOM   5624 H  HD13 . LEU   B 1 108 ? 34.536 -21.963 10.446  1.00 25.85 ?  108 LEU   B HD13 1 
ATOM   5625 H  HD21 . LEU   B 1 108 ? 31.863 -20.837 10.183  1.00 26.66 ?  108 LEU   B HD21 1 
ATOM   5626 H  HD22 . LEU   B 1 108 ? 32.967 -20.564 9.074   1.00 26.66 ?  108 LEU   B HD22 1 
ATOM   5627 H  HD23 . LEU   B 1 108 ? 31.558 -21.172 8.660   1.00 26.66 ?  108 LEU   B HD23 1 
ATOM   5628 N  N    . LEU   B 1 109 ? 33.131 -24.746 5.197   1.00 15.95 ?  109 LEU   B N    1 
ATOM   5629 C  CA   . LEU   B 1 109 ? 33.759 -24.856 3.888   1.00 14.97 ?  109 LEU   B CA   1 
ATOM   5630 C  C    . LEU   B 1 109 ? 32.995 -24.071 2.827   1.00 14.28 ?  109 LEU   B C    1 
ATOM   5631 O  O    . LEU   B 1 109 ? 33.616 -23.474 1.938   1.00 13.73 ?  109 LEU   B O    1 
ATOM   5632 C  CB   . LEU   B 1 109 ? 33.880 -26.330 3.511   1.00 15.01 ?  109 LEU   B CB   1 
ATOM   5633 C  CG   . LEU   B 1 109 ? 34.660 -26.679 2.248   1.00 14.83 ?  109 LEU   B CG   1 
ATOM   5634 C  CD1  . LEU   B 1 109 ? 36.041 -26.028 2.239   1.00 14.45 ?  109 LEU   B CD1  1 
ATOM   5635 C  CD2  . LEU   B 1 109 ? 34.791 -28.191 2.129   1.00 15.54 ?  109 LEU   B CD2  1 
ATOM   5636 H  H    . LEU   B 1 109 ? 32.831 -25.491 5.503   1.00 19.13 ?  109 LEU   B H    1 
ATOM   5637 H  HA   . LEU   B 1 109 ? 34.656 -24.492 3.935   1.00 17.95 ?  109 LEU   B HA   1 
ATOM   5638 H  HB2  . LEU   B 1 109 ? 34.314 -26.797 4.243   1.00 17.99 ?  109 LEU   B HB2  1 
ATOM   5639 H  HB3  . LEU   B 1 109 ? 32.986 -26.691 3.395   1.00 17.99 ?  109 LEU   B HB3  1 
ATOM   5640 H  HG   . LEU   B 1 109 ? 34.172 -26.372 1.468   1.00 17.78 ?  109 LEU   B HG   1 
ATOM   5641 H  HD11 . LEU   B 1 109 ? 36.557 -26.390 1.498   1.00 17.33 ?  109 LEU   B HD11 1 
ATOM   5642 H  HD12 . LEU   B 1 109 ? 35.934 -25.075 2.134   1.00 17.33 ?  109 LEU   B HD12 1 
ATOM   5643 H  HD13 . LEU   B 1 109 ? 36.487 -26.229 3.077   1.00 17.33 ?  109 LEU   B HD13 1 
ATOM   5644 H  HD21 . LEU   B 1 109 ? 35.355 -28.406 1.367   1.00 18.63 ?  109 LEU   B HD21 1 
ATOM   5645 H  HD22 . LEU   B 1 109 ? 35.188 -28.541 2.941   1.00 18.63 ?  109 LEU   B HD22 1 
ATOM   5646 H  HD23 . LEU   B 1 109 ? 33.908 -28.580 2.001   1.00 18.63 ?  109 LEU   B HD23 1 
ATOM   5647 N  N    . LYS   B 1 110 ? 31.659 -24.036 2.904   1.00 14.20 ?  110 LYS   B N    1 
ATOM   5648 C  CA   . LYS   B 1 110 ? 30.905 -23.276 1.912   1.00 13.96 ?  110 LYS   B CA   1 
ATOM   5649 C  C    . LYS   B 1 110 ? 31.246 -21.790 2.001   1.00 13.55 ?  110 LYS   B C    1 
ATOM   5650 O  O    . LYS   B 1 110 ? 31.504 -21.139 0.983   1.00 13.44 ?  110 LYS   B O    1 
ATOM   5651 C  CB   . LYS   B 1 110 ? 29.400 -23.523 2.063   1.00 14.28 ?  110 LYS   B CB   1 
ATOM   5652 C  CG   . LYS   B 1 110 ? 28.590 -22.918 0.920   1.00 14.93 ?  110 LYS   B CG   1 
ATOM   5653 C  CD   . LYS   B 1 110 ? 27.125 -23.341 0.961   1.00 14.93 ?  110 LYS   B CD   1 
ATOM   5654 C  CE   . LYS   B 1 110 ? 26.356 -22.816 -0.250  1.00 15.91 ?  110 LYS   B CE   1 
ATOM   5655 N  NZ   . LYS   B 1 110 ? 26.695 -23.532 -1.506  1.00 16.05 ?  110 LYS   B NZ   1 
ATOM   5656 H  H    . LYS   B 1 110 ? 31.187 -24.436 3.496   1.00 17.02 ?  110 LYS   B H    1 
ATOM   5657 H  HA   . LYS   B 1 110 ? 31.162 -23.581 1.026   1.00 16.73 ?  110 LYS   B HA   1 
ATOM   5658 H  HB2  . LYS   B 1 110 ? 29.237 -24.485 2.071   1.00 17.12 ?  110 LYS   B HB2  1 
ATOM   5659 H  HB3  . LYS   B 1 110 ? 29.094 -23.133 2.894   1.00 17.12 ?  110 LYS   B HB3  1 
ATOM   5660 H  HG2  . LYS   B 1 110 ? 28.619 -21.953 0.986   1.00 17.90 ?  110 LYS   B HG2  1 
ATOM   5661 H  HG3  . LYS   B 1 110 ? 28.958 -23.210 0.075   1.00 17.90 ?  110 LYS   B HG3  1 
ATOM   5662 H  HD2  . LYS   B 1 110 ? 27.069 -24.314 0.960   1.00 17.90 ?  110 LYS   B HD2  1 
ATOM   5663 H  HD3  . LYS   B 1 110 ? 26.707 -22.988 1.765   1.00 17.90 ?  110 LYS   B HD3  1 
ATOM   5664 H  HE2  . LYS   B 1 110 ? 25.405 -22.920 -0.093  1.00 19.08 ?  110 LYS   B HE2  1 
ATOM   5665 H  HE3  . LYS   B 1 110 ? 26.572 -21.878 -0.374  1.00 19.08 ?  110 LYS   B HE3  1 
ATOM   5666 H  HZ1  . LYS   B 1 110 ? 26.232 -23.197 -2.184  1.00 19.24 ?  110 LYS   B HZ1  1 
ATOM   5667 H  HZ2  . LYS   B 1 110 ? 27.566 -23.449 -1.679  1.00 19.24 ?  110 LYS   B HZ2  1 
ATOM   5668 H  HZ3  . LYS   B 1 110 ? 26.502 -24.399 -1.422  1.00 19.24 ?  110 LYS   B HZ3  1 
ATOM   5669 N  N    . SER   B 1 111 ? 31.264 -21.241 3.221   1.00 14.11 ?  111 SER   B N    1 
ATOM   5670 C  CA   . SER   B 1 111 ? 31.655 -19.844 3.403   1.00 13.65 ?  111 SER   B CA   1 
ATOM   5671 C  C    . SER   B 1 111 ? 33.034 -19.583 2.812   1.00 13.04 ?  111 SER   B C    1 
ATOM   5672 O  O    . SER   B 1 111 ? 33.261 -18.548 2.167   1.00 13.24 ?  111 SER   B O    1 
ATOM   5673 C  CB   . SER   B 1 111 ? 31.655 -19.492 4.890   1.00 14.88 ?  111 SER   B CB   1 
ATOM   5674 O  OG   . SER   B 1 111 ? 30.347 -19.483 5.424   1.00 16.46 ?  111 SER   B OG   1 
ATOM   5675 H  H    . SER   B 1 111 ? 31.065 -21.659 3.947   1.00 16.92 ?  111 SER   B H    1 
ATOM   5676 H  HA   . SER   B 1 111 ? 31.017 -19.274 2.955   1.00 16.36 ?  111 SER   B HA   1 
ATOM   5677 H  HB2  . SER   B 1 111 ? 32.174 -20.156 5.373   1.00 17.83 ?  111 SER   B HB2  1 
ATOM   5678 H  HB3  . SER   B 1 111 ? 32.046 -18.617 5.008   1.00 17.83 ?  111 SER   B HB3  1 
ATOM   5679 H  HG   . SER   B 1 111 ? 30.368 -19.280 6.246   1.00 19.73 ?  111 SER   B HG   1 
ATOM   5680 N  N    . ALA   B 1 112 ? 33.971 -20.505 3.032   1.00 13.12 ?  112 ALA   B N    1 
ATOM   5681 C  CA   . ALA   B 1 112 ? 35.316 -20.335 2.492   1.00 12.93 ?  112 ALA   B CA   1 
ATOM   5682 C  C    . ALA   B 1 112 ? 35.290 -20.242 0.968   1.00 12.22 ?  112 ALA   B C    1 
ATOM   5683 O  O    . ALA   B 1 112 ? 35.915 -19.354 0.374   1.00 12.53 ?  112 ALA   B O    1 
ATOM   5684 C  CB   . ALA   B 1 112 ? 36.215 -21.479 2.969   1.00 13.22 ?  112 ALA   B CB   1 
ATOM   5685 H  H    . ALA   B 1 112 ? 33.854 -21.229 3.493   1.00 15.73 ?  112 ALA   B H    1 
ATOM   5686 H  HA   . ALA   B 1 112 ? 35.681 -19.507 2.838   1.00 15.51 ?  112 ALA   B HA   1 
ATOM   5687 H  HB1  . ALA   B 1 112 ? 37.106 -21.344 2.607   1.00 15.85 ?  112 ALA   B HB1  1 
ATOM   5688 H  HB2  . ALA   B 1 112 ? 36.252 -21.469 3.940   1.00 15.85 ?  112 ALA   B HB2  1 
ATOM   5689 H  HB3  . ALA   B 1 112 ? 35.852 -22.319 2.659   1.00 15.85 ?  112 ALA   B HB3  1 
ATOM   5690 N  N    . TYR   B 1 113 ? 34.561 -21.150 0.313   1.00 12.29 ?  113 TYR   B N    1 
ATOM   5691 C  CA   . TYR   B 1 113 ? 34.487 -21.102 -1.143  1.00 12.11 ?  113 TYR   B CA   1 
ATOM   5692 C  C    . TYR   B 1 113 ? 33.776 -19.852 -1.661  1.00 12.00 ?  113 TYR   B C    1 
ATOM   5693 O  O    . TYR   B 1 113 ? 34.040 -19.423 -2.788  1.00 11.88 ?  113 TYR   B O    1 
ATOM   5694 C  CB   . TYR   B 1 113 ? 33.813 -22.357 -1.687  1.00 12.23 ?  113 TYR   B CB   1 
ATOM   5695 C  CG   . TYR   B 1 113 ? 34.775 -23.505 -1.940  1.00 12.74 ?  113 TYR   B CG   1 
ATOM   5696 C  CD1  . TYR   B 1 113 ? 35.779 -23.403 -2.897  1.00 13.47 ?  113 TYR   B CD1  1 
ATOM   5697 C  CD2  . TYR   B 1 113 ? 34.667 -24.696 -1.238  1.00 13.11 ?  113 TYR   B CD2  1 
ATOM   5698 C  CE1  . TYR   B 1 113 ? 36.661 -24.440 -3.134  1.00 13.38 ?  113 TYR   B CE1  1 
ATOM   5699 C  CE2  . TYR   B 1 113 ? 35.543 -25.750 -1.471  1.00 13.34 ?  113 TYR   B CE2  1 
ATOM   5700 C  CZ   . TYR   B 1 113 ? 36.529 -25.619 -2.429  1.00 13.42 ?  113 TYR   B CZ   1 
ATOM   5701 O  OH   . TYR   B 1 113 ? 37.417 -26.642 -2.689  1.00 14.19 ?  113 TYR   B OH   1 
ATOM   5702 H  H    . TYR   B 1 113 ? 34.098 -21.778 0.686   1.00 14.73 ?  113 TYR   B H    1 
ATOM   5703 H  HA   . TYR   B 1 113 ? 35.390 -21.085 -1.480  1.00 14.51 ?  113 TYR   B HA   1 
ATOM   5704 H  HB2  . TYR   B 1 113 ? 33.150 -22.666 -1.043  1.00 14.66 ?  113 TYR   B HB2  1 
ATOM   5705 H  HB3  . TYR   B 1 113 ? 33.376 -22.141 -2.523  1.00 14.66 ?  113 TYR   B HB3  1 
ATOM   5706 H  HD1  . TYR   B 1 113 ? 35.868 -22.609 -3.376  1.00 16.15 ?  113 TYR   B HD1  1 
ATOM   5707 H  HD2  . TYR   B 1 113 ? 33.996 -24.791 -0.604  1.00 15.71 ?  113 TYR   B HD2  1 
ATOM   5708 H  HE1  . TYR   B 1 113 ? 37.327 -24.348 -3.781  1.00 16.04 ?  113 TYR   B HE1  1 
ATOM   5709 H  HE2  . TYR   B 1 113 ? 35.449 -26.548 -0.998  1.00 15.99 ?  113 TYR   B HE2  1 
ATOM   5710 H  HH   . TYR   B 1 113 ? 37.237 -27.308 -2.213  1.00 17.02 ?  113 TYR   B HH   1 
ATOM   5711 N  N    . GLU   B 1 114 ? 32.851 -19.275 -0.885  1.00 12.12 ?  114 GLU   B N    1 
ATOM   5712 C  CA   . GLU   B 1 114 ? 32.171 -18.061 -1.335  1.00 11.96 ?  114 GLU   B CA   1 
ATOM   5713 C  C    . GLU   B 1 114 ? 33.155 -16.941 -1.636  1.00 11.66 ?  114 GLU   B C    1 
ATOM   5714 O  O    . GLU   B 1 114 ? 32.872 -16.079 -2.473  1.00 11.90 ?  114 GLU   B O    1 
ATOM   5715 C  CB   . GLU   B 1 114 ? 31.111 -17.637 -0.314  1.00 12.55 ?  114 GLU   B CB   1 
ATOM   5716 C  CG   . GLU   B 1 114 ? 29.889 -18.556 -0.384  1.00 12.67 ?  114 GLU   B CG   1 
ATOM   5717 C  CD   . GLU   B 1 114 ? 28.869 -18.365 0.722   1.00 13.07 ?  114 GLU   B CD   1 
ATOM   5718 O  OE1  . GLU   B 1 114 ? 29.157 -17.747 1.762   1.00 13.24 ?  114 GLU   B OE1  1 
ATOM   5719 O  OE2  . GLU   B 1 114 ? 27.746 -18.904 0.559   1.00 14.06 -1 114 GLU   B OE2  1 
ATOM   5720 H  H    . GLU   B 1 114 ? 32.594 -19.573 -0.115  1.00 14.53 ?  114 GLU   B H    1 
ATOM   5721 H  HA   . GLU   B 1 114 ? 31.710 -18.262 -2.160  1.00 14.34 ?  114 GLU   B HA   1 
ATOM   5722 H  HB2  . GLU   B 1 114 ? 31.483 -17.692 0.581   1.00 15.04 ?  114 GLU   B HB2  1 
ATOM   5723 H  HB3  . GLU   B 1 114 ? 30.823 -16.733 -0.506  1.00 15.04 ?  114 GLU   B HB3  1 
ATOM   5724 H  HG2  . GLU   B 1 114 ? 29.441 -18.405 -1.227  1.00 15.19 ?  114 GLU   B HG2  1 
ATOM   5725 H  HG3  . GLU   B 1 114 ? 30.196 -19.476 -0.337  1.00 15.19 ?  114 GLU   B HG3  1 
ATOM   5726 N  N    . ASN   B 1 115 ? 34.322 -16.939 -0.989  1.00 11.53 ?  115 ASN   B N    1 
ATOM   5727 C  CA   . ASN   B 1 115 ? 35.312 -15.907 -1.287  1.00 11.22 ?  115 ASN   B CA   1 
ATOM   5728 C  C    . ASN   B 1 115 ? 35.723 -15.928 -2.752  1.00 11.11 ?  115 ASN   B C    1 
ATOM   5729 O  O    . ASN   B 1 115 ? 36.111 -14.888 -3.307  1.00 11.84 ?  115 ASN   B O    1 
ATOM   5730 C  CB   . ASN   B 1 115 ? 36.548 -16.076 -0.400  1.00 12.06 ?  115 ASN   B CB   1 
ATOM   5731 C  CG   . ASN   B 1 115 ? 36.273 -15.809 1.061   1.00 12.60 ?  115 ASN   B CG   1 
ATOM   5732 O  OD1  . ASN   B 1 115 ? 36.280 -14.662 1.501   1.00 14.70 ?  115 ASN   B OD1  1 
ATOM   5733 N  ND2  . ASN   B 1 115 ? 36.108 -16.873 1.839   1.00 12.47 ?  115 ASN   B ND2  1 
ATOM   5734 H  H    . ASN   B 1 115 ? 34.563 -17.506 -0.380  1.00 13.82 ?  115 ASN   B H    1 
ATOM   5735 H  HA   . ASN   B 1 115 ? 34.931 -15.038 -1.100  1.00 13.45 ?  115 ASN   B HA   1 
ATOM   5736 H  HB2  . ASN   B 1 115 ? 36.881 -16.982 -0.484  1.00 14.45 ?  115 ASN   B HB2  1 
ATOM   5737 H  HB3  . ASN   B 1 115 ? 37.233 -15.448 -0.689  1.00 14.45 ?  115 ASN   B HB3  1 
ATOM   5738 H  HD21 . ASN   B 1 115 ? 35.962 -16.775 2.681   1.00 14.95 ?  115 ASN   B HD21 1 
ATOM   5739 H  HD22 . ASN   B 1 115 ? 36.134 -17.665 1.500   1.00 14.95 ?  115 ASN   B HD22 1 
ATOM   5740 N  N    . PHE   B 1 116 ? 35.694 -17.106 -3.386  1.00 11.07 ?  116 PHE   B N    1 
ATOM   5741 C  CA   . PHE   B 1 116 ? 36.127 -17.197 -4.775  1.00 11.54 ?  116 PHE   B CA   1 
ATOM   5742 C  C    . PHE   B 1 116 ? 35.225 -16.373 -5.691  1.00 11.33 ?  116 PHE   B C    1 
ATOM   5743 O  O    . PHE   B 1 116 ? 35.659 -15.951 -6.769  1.00 11.89 ?  116 PHE   B O    1 
ATOM   5744 C  CB   . PHE   B 1 116 ? 36.090 -18.644 -5.290  1.00 11.01 ?  116 PHE   B CB   1 
ATOM   5745 C  CG   . PHE   B 1 116 ? 37.162 -19.600 -4.739  1.00 10.82 ?  116 PHE   B CG   1 
ATOM   5746 C  CD1  . PHE   B 1 116 ? 37.798 -19.424 -3.522  1.00 11.89 ?  116 PHE   B CD1  1 
ATOM   5747 C  CD2  . PHE   B 1 116 ? 37.467 -20.738 -5.474  1.00 11.32 ?  116 PHE   B CD2  1 
ATOM   5748 C  CE1  . PHE   B 1 116 ? 38.740 -20.361 -3.067  1.00 11.96 ?  116 PHE   B CE1  1 
ATOM   5749 C  CE2  . PHE   B 1 116 ? 38.398 -21.673 -5.027  1.00 11.59 ?  116 PHE   B CE2  1 
ATOM   5750 C  CZ   . PHE   B 1 116 ? 39.023 -21.494 -3.824  1.00 11.72 ?  116 PHE   B CZ   1 
ATOM   5751 H  H    . PHE   B 1 116 ? 35.433 -17.853 -3.039  1.00 13.27 ?  116 PHE   B H    1 
ATOM   5752 H  HA   . PHE   B 1 116 ? 37.036 -16.871 -4.856  1.00 13.84 ?  116 PHE   B HA   1 
ATOM   5753 H  HB2  . PHE   B 1 116 ? 35.219 -19.023 -5.064  1.00 13.19 ?  116 PHE   B HB2  1 
ATOM   5754 H  HB3  . PHE   B 1 116 ? 36.184 -18.627 -6.255  1.00 13.19 ?  116 PHE   B HB3  1 
ATOM   5755 H  HD1  . PHE   B 1 116 ? 37.595 -18.676 -3.003  1.00 14.25 ?  116 PHE   B HD1  1 
ATOM   5756 H  HD2  . PHE   B 1 116 ? 37.038 -20.882 -6.287  1.00 13.57 ?  116 PHE   B HD2  1 
ATOM   5757 H  HE1  . PHE   B 1 116 ? 39.164 -20.228 -2.250  1.00 14.33 ?  116 PHE   B HE1  1 
ATOM   5758 H  HE2  . PHE   B 1 116 ? 38.589 -22.417 -5.545  1.00 13.90 ?  116 PHE   B HE2  1 
ATOM   5759 H  HZ   . PHE   B 1 116 ? 39.659 -22.103 -3.529  1.00 14.05 ?  116 PHE   B HZ   1 
ATOM   5760 N  N    . ASN   B 1 117 ? 33.959 -16.172 -5.309  1.00 11.70 ?  117 ASN   B N    1 
ATOM   5761 C  CA   . ASN   B 1 117 ? 33.010 -15.472 -6.172  1.00 11.91 ?  117 ASN   B CA   1 
ATOM   5762 C  C    . ASN   B 1 117 ? 33.325 -13.993 -6.326  1.00 12.16 ?  117 ASN   B C    1 
ATOM   5763 O  O    . ASN   B 1 117 ? 32.724 -13.341 -7.183  1.00 13.47 ?  117 ASN   B O    1 
ATOM   5764 C  CB   . ASN   B 1 117 ? 31.586 -15.690 -5.669  1.00 12.03 ?  117 ASN   B CB   1 
ATOM   5765 C  CG   . ASN   B 1 117 ? 31.125 -17.098 -5.922  1.00 12.49 ?  117 ASN   B CG   1 
ATOM   5766 O  OD1  . ASN   B 1 117 ? 31.481 -17.694 -6.940  1.00 13.44 ?  117 ASN   B OD1  1 
ATOM   5767 N  ND2  . ASN   B 1 117 ? 30.386 -17.668 -4.982  1.00 12.44 ?  117 ASN   B ND2  1 
ATOM   5768 H  H    . ASN   B 1 117 ? 33.633 -16.430 -4.552  1.00 14.03 ?  117 ASN   B H    1 
ATOM   5769 H  HA   . ASN   B 1 117 ? 33.066 -15.871 -7.050  1.00 14.28 ?  117 ASN   B HA   1 
ATOM   5770 H  HB2  . ASN   B 1 117 ? 31.557 -15.525 -4.710  1.00 14.42 ?  117 ASN   B HB2  1 
ATOM   5771 H  HB3  . ASN   B 1 117 ? 30.991 -15.078 -6.129  1.00 14.42 ?  117 ASN   B HB3  1 
ATOM   5772 H  HD21 . ASN   B 1 117 ? 30.103 -18.474 -5.087  1.00 14.91 ?  117 ASN   B HD21 1 
ATOM   5773 H  HD22 . ASN   B 1 117 ? 30.169 -17.225 -4.277  1.00 14.91 ?  117 ASN   B HD22 1 
ATOM   5774 N  N    . GLN   B 1 118 ? 34.265 -13.466 -5.553  1.00 11.91 ?  118 GLN   B N    1 
ATOM   5775 C  CA   . GLN   B 1 118 ? 34.691 -12.080 -5.688  1.00 12.68 ?  118 GLN   B CA   1 
ATOM   5776 C  C    . GLN   B 1 118 ? 35.759 -11.886 -6.759  1.00 12.69 ?  118 GLN   B C    1 
ATOM   5777 O  O    . GLN   B 1 118 ? 36.234 -10.762 -6.941  1.00 13.95 ?  118 GLN   B O    1 
ATOM   5778 C  CB   . GLN   B 1 118 ? 35.170 -11.543 -4.333  1.00 13.08 ?  118 GLN   B CB   1 
ATOM   5779 C  CG   . GLN   B 1 118 ? 34.087 -11.580 -3.263  1.00 13.13 ?  118 GLN   B CG   1 
ATOM   5780 C  CD   . GLN   B 1 118 ? 32.913 -10.670 -3.592  1.00 13.18 ?  118 GLN   B CD   1 
ATOM   5781 O  OE1  . GLN   B 1 118 ? 33.100 -9.533  -4.031  1.00 14.04 ?  118 GLN   B OE1  1 
ATOM   5782 N  NE2  . GLN   B 1 118 ? 31.699 -11.166 -3.386  1.00 13.70 ?  118 GLN   B NE2  1 
ATOM   5783 H  H    . GLN   B 1 118 ? 34.695 -13.894 -4.937  1.00 14.27 ?  118 GLN   B H    1 
ATOM   5784 H  HA   . GLN   B 1 118 ? 33.927 -11.549 -5.963  1.00 15.20 ?  118 GLN   B HA   1 
ATOM   5785 H  HB2  . GLN   B 1 118 ? 35.915 -12.072 -4.026  1.00 15.68 ?  118 GLN   B HB2  1 
ATOM   5786 H  HB3  . GLN   B 1 118 ? 35.444 -10.613 -4.440  1.00 15.68 ?  118 GLN   B HB3  1 
ATOM   5787 H  HG2  . GLN   B 1 118 ? 33.756 -12.489 -3.183  1.00 15.74 ?  118 GLN   B HG2  1 
ATOM   5788 H  HG3  . GLN   B 1 118 ? 34.468 -11.291 -2.419  1.00 15.74 ?  118 GLN   B HG3  1 
ATOM   5789 H  HE21 . GLN   B 1 118 ? 31.610 -11.965 -3.075  1.00 16.42 ?  118 GLN   B HE21 1 
ATOM   5790 H  HE22 . GLN   B 1 118 ? 31.009 -10.690 -3.557  1.00 16.42 ?  118 GLN   B HE22 1 
ATOM   5791 N  N    . HIS   B 1 119 ? 36.110 -12.944 -7.493  1.00 12.12 ?  119 HIS   B N    1 
ATOM   5792 C  CA   . HIS   B 1 119 ? 37.151 -12.901 -8.510  1.00 12.50 ?  119 HIS   B CA   1 
ATOM   5793 C  C    . HIS   B 1 119 ? 36.672 -13.638 -9.746  1.00 12.15 ?  119 HIS   B C    1 
ATOM   5794 O  O    . HIS   B 1 119 ? 36.159 -14.753 -9.641  1.00 12.88 ?  119 HIS   B O    1 
ATOM   5795 C  CB   . HIS   B 1 119 ? 38.429 -13.533 -7.958  1.00 13.01 ?  119 HIS   B CB   1 
ATOM   5796 C  CG   . HIS   B 1 119 ? 38.913 -12.836 -6.731  1.00 14.05 ?  119 HIS   B CG   1 
ATOM   5797 N  ND1  . HIS   B 1 119 ? 39.711 -11.713 -6.784  1.00 15.38 ?  119 HIS   B ND1  1 
ATOM   5798 C  CD2  . HIS   B 1 119 ? 38.625 -13.038 -5.425  1.00 15.11 ?  119 HIS   B CD2  1 
ATOM   5799 C  CE1  . HIS   B 1 119 ? 39.924 -11.278 -5.556  1.00 16.70 ?  119 HIS   B CE1  1 
ATOM   5800 N  NE2  . HIS   B 1 119 ? 39.269 -12.057 -4.714  1.00 16.62 ?  119 HIS   B NE2  1 
ATOM   5801 H  H    . HIS   B 1 119 ? 35.736 -13.719 -7.427  1.00 14.53 ?  119 HIS   B H    1 
ATOM   5802 H  HA   . HIS   B 1 119 ? 37.335 -11.978 -8.752  1.00 14.99 ?  119 HIS   B HA   1 
ATOM   5803 H  HB2  . HIS   B 1 119 ? 38.253 -14.459 -7.734  1.00 15.60 ?  119 HIS   B HB2  1 
ATOM   5804 H  HB3  . HIS   B 1 119 ? 39.126 -13.479 -8.633  1.00 15.60 ?  119 HIS   B HB3  1 
ATOM   5805 H  HD2  . HIS   B 1 119 ? 38.092 -13.718 -5.075  1.00 18.12 ?  119 HIS   B HD2  1 
ATOM   5806 H  HE1  . HIS   B 1 119 ? 40.454 -10.552 -5.318  1.00 20.02 ?  119 HIS   B HE1  1 
ATOM   5807 H  HE2  . HIS   B 1 119 ? 39.276 -11.985 -3.855  1.00 19.93 ?  119 HIS   B HE2  1 
ATOM   5808 N  N    . GLU   B 1 120 ? 36.831 -13.021 -10.918 1.00 12.82 ?  120 GLU   B N    1 
ATOM   5809 C  CA   . GLU   B 1 120 ? 36.244 -13.603 -12.122 1.00 14.47 ?  120 GLU   B CA   1 
ATOM   5810 C  C    . GLU   B 1 120 ? 36.914 -14.909 -12.528 1.00 13.43 ?  120 GLU   B C    1 
ATOM   5811 O  O    . GLU   B 1 120 ? 36.249 -15.782 -13.096 1.00 13.76 ?  120 GLU   B O    1 
ATOM   5812 C  CB   . GLU   B 1 120 ? 36.268 -12.599 -13.272 1.00 18.82 ?  120 GLU   B CB   1 
ATOM   5813 C  CG   . GLU   B 1 120 ? 35.301 -11.447 -13.075 1.00 25.11 ?  120 GLU   B CG   1 
ATOM   5814 C  CD   . GLU   B 1 120 ? 35.199 -10.544 -14.289 1.00 30.88 ?  120 GLU   B CD   1 
ATOM   5815 O  OE1  . GLU   B 1 120 ? 36.207 -10.397 -15.013 1.00 33.39 ?  120 GLU   B OE1  1 
ATOM   5816 O  OE2  . GLU   B 1 120 ? 34.106 -9.984  -14.518 1.00 33.83 -1 120 GLU   B OE2  1 
ATOM   5817 H  H    . GLU   B 1 120 ? 37.257 -12.282 -11.043 1.00 15.37 ?  120 GLU   B H    1 
ATOM   5818 H  HA   . GLU   B 1 120 ? 35.317 -13.807 -11.939 1.00 17.35 ?  120 GLU   B HA   1 
ATOM   5819 H  HB2  . GLU   B 1 120 ? 37.158 -12.226 -13.353 1.00 22.57 ?  120 GLU   B HB2  1 
ATOM   5820 H  HB3  . GLU   B 1 120 ? 36.022 -13.052 -14.095 1.00 22.57 ?  120 GLU   B HB3  1 
ATOM   5821 H  HG2  . GLU   B 1 120 ? 34.413 -11.800 -12.900 1.00 30.11 ?  120 GLU   B HG2  1 
ATOM   5822 H  HG3  . GLU   B 1 120 ? 35.595 -10.907 -12.326 1.00 30.11 ?  120 GLU   B HG3  1 
ATOM   5823 N  N    . VAL   B 1 121 ? 38.215 -15.052 -12.269 1.00 13.05 ?  121 VAL   B N    1 
ATOM   5824 C  CA   . VAL   B 1 121 ? 38.961 -16.261 -12.616 1.00 12.54 ?  121 VAL   B CA   1 
ATOM   5825 C  C    . VAL   B 1 121 ? 40.074 -16.460 -11.596 1.00 12.14 ?  121 VAL   B C    1 
ATOM   5826 O  O    . VAL   B 1 121 ? 40.753 -15.500 -11.207 1.00 12.83 ?  121 VAL   B O    1 
ATOM   5827 C  CB   . VAL   B 1 121 ? 39.474 -16.214 -14.073 1.00 14.30 ?  121 VAL   B CB   1 
ATOM   5828 C  CG1  . VAL   B 1 121 ? 40.339 -14.982 -14.318 1.00 15.78 ?  121 VAL   B CG1  1 
ATOM   5829 C  CG2  . VAL   B 1 121 ? 40.221 -17.497 -14.429 1.00 15.71 ?  121 VAL   B CG2  1 
ATOM   5830 H  H    . VAL   B 1 121 ? 38.701 -14.451 -11.894 1.00 15.65 ?  121 VAL   B H    1 
ATOM   5831 H  HA   . VAL   B 1 121 ? 38.354 -17.018 -12.548 1.00 15.04 ?  121 VAL   B HA   1 
ATOM   5832 H  HB   . VAL   B 1 121 ? 38.707 -16.156 -14.669 1.00 17.14 ?  121 VAL   B HB   1 
ATOM   5833 H  HG11 . VAL   B 1 121 ? 40.650 -14.991 -15.237 1.00 18.92 ?  121 VAL   B HG11 1 
ATOM   5834 H  HG12 . VAL   B 1 121 ? 39.808 -14.186 -14.157 1.00 18.92 ?  121 VAL   B HG12 1 
ATOM   5835 H  HG13 . VAL   B 1 121 ? 41.096 -15.003 -13.712 1.00 18.92 ?  121 VAL   B HG13 1 
ATOM   5836 H  HG21 . VAL   B 1 121 ? 40.426 -17.491 -15.380 1.00 18.84 ?  121 VAL   B HG21 1 
ATOM   5837 H  HG22 . VAL   B 1 121 ? 41.045 -17.538 -13.919 1.00 18.84 ?  121 VAL   B HG22 1 
ATOM   5838 H  HG23 . VAL   B 1 121 ? 39.663 -18.262 -14.221 1.00 18.84 ?  121 VAL   B HG23 1 
ATOM   5839 N  N    . LEU   B 1 122 ? 40.253 -17.712 -11.156 1.00 11.62 ?  122 LEU   B N    1 
ATOM   5840 C  CA   . LEU   B 1 122 ? 41.236 -18.063 -10.135 1.00 11.26 ?  122 LEU   B CA   1 
ATOM   5841 C  C    . LEU   B 1 122 ? 41.889 -19.395 -10.456 1.00 11.31 ?  122 LEU   B C    1 
ATOM   5842 O  O    . LEU   B 1 122 ? 41.229 -20.318 -10.950 1.00 12.37 ?  122 LEU   B O    1 
ATOM   5843 C  CB   . LEU   B 1 122 ? 40.589 -18.294 -8.754  1.00 13.17 ?  122 LEU   B CB   1 
ATOM   5844 C  CG   . LEU   B 1 122 ? 39.557 -17.270 -8.268  1.00 13.34 ?  122 LEU   B CG   1 
ATOM   5845 C  CD1  . LEU   B 1 122 ? 38.162 -17.630 -8.754  1.00 14.14 ?  122 LEU   B CD1  1 
ATOM   5846 C  CD2  . LEU   B 1 122 ? 39.593 -17.157 -6.757  1.00 12.65 ?  122 LEU   B CD2  1 
ATOM   5847 H  H    . LEU   B 1 122 ? 39.806 -18.391 -11.442 1.00 13.93 ?  122 LEU   B H    1 
ATOM   5848 H  HA   . LEU   B 1 122 ? 41.913 -17.371 -10.058 1.00 13.50 ?  122 LEU   B HA   1 
ATOM   5849 H  HB2  . LEU   B 1 122 ? 40.143 -19.153 -8.771  1.00 15.79 ?  122 LEU   B HB2  1 
ATOM   5850 H  HB3  . LEU   B 1 122 ? 41.295 -18.313 -8.090  1.00 15.79 ?  122 LEU   B HB3  1 
ATOM   5851 H  HG   . LEU   B 1 122 ? 39.783 -16.401 -8.633  1.00 15.99 ?  122 LEU   B HG   1 
ATOM   5852 H  HD11 . LEU   B 1 122 ? 37.528 -16.993 -8.385  1.00 16.95 ?  122 LEU   B HD11 1 
ATOM   5853 H  HD12 . LEU   B 1 122 ? 38.143 -17.582 -9.724  1.00 16.95 ?  122 LEU   B HD12 1 
ATOM   5854 H  HD13 . LEU   B 1 122 ? 37.943 -18.524 -8.460  1.00 16.95 ?  122 LEU   B HD13 1 
ATOM   5855 H  HD21 . LEU   B 1 122 ? 38.913 -16.526 -6.470  1.00 15.16 ?  122 LEU   B HD21 1 
ATOM   5856 H  HD22 . LEU   B 1 122 ? 39.419 -18.029 -6.369  1.00 15.16 ?  122 LEU   B HD22 1 
ATOM   5857 H  HD23 . LEU   B 1 122 ? 40.470 -16.843 -6.483  1.00 15.16 ?  122 LEU   B HD23 1 
ATOM   5858 N  N    . LEU   B 1 123 ? 43.176 -19.504 -10.100 1.00 10.93 ?  123 LEU   B N    1 
ATOM   5859 C  CA   . LEU   B 1 123 ? 43.886 -20.772 -9.976  1.00 11.16 ?  123 LEU   B CA   1 
ATOM   5860 C  C    . LEU   B 1 123 ? 43.861 -21.165 -8.504  1.00 10.93 ?  123 LEU   B C    1 
ATOM   5861 O  O    . LEU   B 1 123 ? 44.208 -20.339 -7.652  1.00 11.09 ?  123 LEU   B O    1 
ATOM   5862 C  CB   . LEU   B 1 123 ? 45.333 -20.596 -10.440 1.00 11.76 ?  123 LEU   B CB   1 
ATOM   5863 C  CG   . LEU   B 1 123 ? 46.280 -21.778 -10.199 1.00 12.07 ?  123 LEU   B CG   1 
ATOM   5864 C  CD1  . LEU   B 1 123 ? 45.865 -23.023 -10.984 1.00 12.67 ?  123 LEU   B CD1  1 
ATOM   5865 C  CD2  . LEU   B 1 123 ? 47.698 -21.366 -10.562 1.00 13.02 ?  123 LEU   B CD2  1 
ATOM   5866 H  H    . LEU   B 1 123 ? 43.672 -18.825 -9.907  1.00 13.10 ?  123 LEU   B H    1 
ATOM   5867 H  HA   . LEU   B 1 123 ? 43.446 -21.462 -10.501 1.00 13.37 ?  123 LEU   B HA   1 
ATOM   5868 H  HB2  . LEU   B 1 123 ? 45.318 -20.428 -11.394 1.00 14.09 ?  123 LEU   B HB2  1 
ATOM   5869 H  HB3  . LEU   B 1 123 ? 45.703 -19.831 -9.981  1.00 14.09 ?  123 LEU   B HB3  1 
ATOM   5870 H  HG   . LEU   B 1 123 ? 46.273 -22.007 -9.256  1.00 14.47 ?  123 LEU   B HG   1 
ATOM   5871 H  HD11 . LEU   B 1 123 ? 46.501 -23.733 -10.805 1.00 15.19 ?  123 LEU   B HD11 1 
ATOM   5872 H  HD12 . LEU   B 1 123 ? 44.978 -23.293 -10.700 1.00 15.19 ?  123 LEU   B HD12 1 
ATOM   5873 H  HD13 . LEU   B 1 123 ? 45.861 -22.811 -11.930 1.00 15.19 ?  123 LEU   B HD13 1 
ATOM   5874 H  HD21 . LEU   B 1 123 ? 48.292 -22.115 -10.411 1.00 15.61 ?  123 LEU   B HD21 1 
ATOM   5875 H  HD22 . LEU   B 1 123 ? 47.719 -21.107 -11.497 1.00 15.61 ?  123 LEU   B HD22 1 
ATOM   5876 H  HD23 . LEU   B 1 123 ? 47.958 -20.616 -10.005 1.00 15.61 ?  123 LEU   B HD23 1 
ATOM   5877 N  N    . ALA   B 1 124 ? 43.432 -22.397 -8.196  1.00 10.96 ?  124 ALA   B N    1 
ATOM   5878 C  CA   . ALA   B 1 124 ? 43.172 -22.715 -6.800  1.00 11.21 ?  124 ALA   B CA   1 
ATOM   5879 C  C    . ALA   B 1 124 ? 43.444 -24.174 -6.467  1.00 10.95 ?  124 ALA   B C    1 
ATOM   5880 O  O    . ALA   B 1 124 ? 43.303 -25.053 -7.330  1.00 11.37 ?  124 ALA   B O    1 
ATOM   5881 C  CB   . ALA   B 1 124 ? 41.714 -22.401 -6.429  1.00 11.52 ?  124 ALA   B CB   1 
ATOM   5882 H  H    . ALA   B 1 124 ? 43.276 -23.039 -8.754  1.00 13.14 ?  124 ALA   B H    1 
ATOM   5883 H  HA   . ALA   B 1 124 ? 43.740 -22.161 -6.251  1.00 13.44 ?  124 ALA   B HA   1 
ATOM   5884 H  HB1  . ALA   B 1 124 ? 41.562 -22.619 -5.496  1.00 13.80 ?  124 ALA   B HB1  1 
ATOM   5885 H  HB2  . ALA   B 1 124 ? 41.545 -21.454 -6.576  1.00 13.80 ?  124 ALA   B HB2  1 
ATOM   5886 H  HB3  . ALA   B 1 124 ? 41.119 -22.928 -6.990  1.00 13.80 ?  124 ALA   B HB3  1 
ATOM   5887 N  N    . PRO   B 1 125 ? 43.741 -24.461 -5.203  1.00 11.09 ?  125 PRO   B N    1 
ATOM   5888 C  CA   . PRO   B 1 125 ? 43.679 -25.825 -4.676  1.00 11.61 ?  125 PRO   B CA   1 
ATOM   5889 C  C    . PRO   B 1 125 ? 42.280 -26.101 -4.127  1.00 11.61 ?  125 PRO   B C    1 
ATOM   5890 O  O    . PRO   B 1 125 ? 41.483 -25.185 -3.924  1.00 12.13 ?  125 PRO   B O    1 
ATOM   5891 C  CB   . PRO   B 1 125 ? 44.663 -25.748 -3.505  1.00 12.76 ?  125 PRO   B CB   1 
ATOM   5892 C  CG   . PRO   B 1 125 ? 44.413 -24.366 -2.938  1.00 12.67 ?  125 PRO   B CG   1 
ATOM   5893 C  CD   . PRO   B 1 125 ? 44.058 -23.490 -4.140  1.00 11.72 ?  125 PRO   B CD   1 
ATOM   5894 H  HA   . PRO   B 1 125 ? 43.953 -26.496 -5.322  1.00 13.92 ?  125 PRO   B HA   1 
ATOM   5895 H  HB2  . PRO   B 1 125 ? 44.458 -26.433 -2.846  1.00 15.30 ?  125 PRO   B HB2  1 
ATOM   5896 H  HB3  . PRO   B 1 125 ? 45.575 -25.834 -3.823  1.00 15.30 ?  125 PRO   B HB3  1 
ATOM   5897 H  HG2  . PRO   B 1 125 ? 43.676 -24.391 -2.307  1.00 15.19 ?  125 PRO   B HG2  1 
ATOM   5898 H  HG3  . PRO   B 1 125 ? 45.219 -24.036 -2.500  1.00 15.19 ?  125 PRO   B HG3  1 
ATOM   5899 H  HD2  . PRO   B 1 125 ? 43.286 -22.939 -3.946  1.00 14.05 ?  125 PRO   B HD2  1 
ATOM   5900 H  HD3  . PRO   B 1 125 ? 44.825 -22.943 -4.396  1.00 14.05 ?  125 PRO   B HD3  1 
ATOM   5901 N  N    . LEU   B 1 126 ? 42.011 -27.377 -3.844  1.00 12.40 ?  126 LEU   B N    1 
ATOM   5902 C  CA   . LEU   B 1 126 ? 40.792 -27.745 -3.128  1.00 12.97 ?  126 LEU   B CA   1 
ATOM   5903 C  C    . LEU   B 1 126 ? 40.908 -27.343 -1.665  1.00 13.25 ?  126 LEU   B C    1 
ATOM   5904 O  O    . LEU   B 1 126 ? 41.800 -27.806 -0.950  1.00 14.89 ?  126 LEU   B O    1 
ATOM   5905 C  CB   . LEU   B 1 126 ? 40.537 -29.243 -3.241  1.00 14.31 ?  126 LEU   B CB   1 
ATOM   5906 C  CG   . LEU   B 1 126 ? 40.008 -29.729 -4.592  1.00 15.31 ?  126 LEU   B CG   1 
ATOM   5907 C  CD1  . LEU   B 1 126 ? 40.059 -31.238 -4.673  1.00 17.27 ?  126 LEU   B CD1  1 
ATOM   5908 C  CD2  . LEU   B 1 126 ? 38.586 -29.248 -4.835  1.00 15.62 ?  126 LEU   B CD2  1 
ATOM   5909 H  H    . LEU   B 1 126 ? 42.520 -28.041 -4.041  1.00 14.87 ?  126 LEU   B H    1 
ATOM   5910 H  HA   . LEU   B 1 126 ? 40.041 -27.271 -3.512  1.00 15.55 ?  126 LEU   B HA   1 
ATOM   5911 H  HB2  . LEU   B 1 126 ? 41.369 -29.707 -3.069  1.00 17.16 ?  126 LEU   B HB2  1 
ATOM   5912 H  HB3  . LEU   B 1 126 ? 39.882 -29.490 -2.569  1.00 17.16 ?  126 LEU   B HB3  1 
ATOM   5913 H  HG   . LEU   B 1 126 ? 40.572 -29.373 -5.298  1.00 18.36 ?  126 LEU   B HG   1 
ATOM   5914 H  HD11 . LEU   B 1 126 ? 39.720 -31.519 -5.538  1.00 20.71 ?  126 LEU   B HD11 1 
ATOM   5915 H  HD12 . LEU   B 1 126 ? 40.975 -31.532 -4.564  1.00 20.71 ?  126 LEU   B HD12 1 
ATOM   5916 H  HD13 . LEU   B 1 126 ? 39.505 -31.610 -3.967  1.00 20.71 ?  126 LEU   B HD13 1 
ATOM   5917 H  HD21 . LEU   B 1 126 ? 38.253 -29.653 -5.652  1.00 18.73 ?  126 LEU   B HD21 1 
ATOM   5918 H  HD22 . LEU   B 1 126 ? 38.032 -29.511 -4.085  1.00 18.73 ?  126 LEU   B HD22 1 
ATOM   5919 H  HD23 . LEU   B 1 126 ? 38.590 -28.282 -4.923  1.00 18.73 ?  126 LEU   B HD23 1 
ATOM   5920 N  N    . LEU   B 1 127 ? 39.978 -26.510 -1.207  1.00 12.99 ?  127 LEU   B N    1 
ATOM   5921 C  CA   . LEU   B 1 127 ? 40.031 -26.017 0.157   1.00 13.51 ?  127 LEU   B CA   1 
ATOM   5922 C  C    . LEU   B 1 127 ? 39.758 -27.136 1.152   1.00 13.38 ?  127 LEU   B C    1 
ATOM   5923 O  O    . LEU   B 1 127 ? 38.935 -28.032 0.921   1.00 13.79 ?  127 LEU   B O    1 
ATOM   5924 C  CB   . LEU   B 1 127 ? 39.014 -24.891 0.361   1.00 14.02 ?  127 LEU   B CB   1 
ATOM   5925 C  CG   . LEU   B 1 127 ? 39.193 -23.626 -0.480  1.00 14.72 ?  127 LEU   B CG   1 
ATOM   5926 C  CD1  . LEU   B 1 127 ? 38.068 -22.656 -0.156  1.00 14.79 ?  127 LEU   B CD1  1 
ATOM   5927 C  CD2  . LEU   B 1 127 ? 40.555 -22.976 -0.254  1.00 15.37 ?  127 LEU   B CD2  1 
ATOM   5928 H  H    . LEU   B 1 127 ? 39.314 -26.210 -1.668  1.00 15.57 ?  127 LEU   B H    1 
ATOM   5929 H  HA   . LEU   B 1 127 ? 40.918 -25.657 0.334   1.00 16.20 ?  127 LEU   B HA   1 
ATOM   5930 H  HB2  . LEU   B 1 127 ? 38.132 -25.244 0.163   1.00 16.81 ?  127 LEU   B HB2  1 
ATOM   5931 H  HB3  . LEU   B 1 127 ? 39.045 -24.620 1.292   1.00 16.81 ?  127 LEU   B HB3  1 
ATOM   5932 H  HG   . LEU   B 1 127 ? 39.114 -23.856 -1.415  1.00 17.65 ?  127 LEU   B HG   1 
ATOM   5933 H  HD11 . LEU   B 1 127 ? 38.185 -21.846 -0.684  1.00 17.73 ?  127 LEU   B HD11 1 
ATOM   5934 H  HD12 . LEU   B 1 127 ? 37.215 -23.064 -0.370  1.00 17.73 ?  127 LEU   B HD12 1 
ATOM   5935 H  HD13 . LEU   B 1 127 ? 38.098 -22.433 0.790   1.00 17.73 ?  127 LEU   B HD13 1 
ATOM   5936 H  HD21 . LEU   B 1 127 ? 40.586 -22.135 -0.735  1.00 18.43 ?  127 LEU   B HD21 1 
ATOM   5937 H  HD22 . LEU   B 1 127 ? 40.677 -22.819 0.696   1.00 18.43 ?  127 LEU   B HD22 1 
ATOM   5938 H  HD23 . LEU   B 1 127 ? 41.242 -23.574 -0.582  1.00 18.43 ?  127 LEU   B HD23 1 
ATOM   5939 N  N    . SER   B 1 128 ? 40.442 -27.054 2.284   1.00 13.41 ?  128 SER   B N    1 
ATOM   5940 C  CA   . SER   B 1 128 ? 40.321 -27.970 3.404   1.00 13.96 ?  128 SER   B CA   1 
ATOM   5941 C  C    . SER   B 1 128 ? 40.806 -29.380 3.082   1.00 15.38 ?  128 SER   B C    1 
ATOM   5942 O  O    . SER   B 1 128 ? 40.703 -30.260 3.935   1.00 16.74 ?  128 SER   B O    1 
ATOM   5943 C  CB   . SER   B 1 128 ? 38.917 -27.972 4.023   1.00 14.40 ?  128 SER   B CB   1 
ATOM   5944 O  OG   . SER   B 1 128 ? 38.615 -26.697 4.572   1.00 14.89 ?  128 SER   B OG   1 
ATOM   5945 H  H    . SER   B 1 128 ? 41.013 -26.426 2.435   1.00 16.08 ?  128 SER   B H    1 
ATOM   5946 H  HA   . SER   B 1 128 ? 40.906 -27.642 4.092   1.00 16.74 ?  128 SER   B HA   1 
ATOM   5947 H  HB2  . SER   B 1 128 ? 38.261 -28.194 3.341   1.00 17.26 ?  128 SER   B HB2  1 
ATOM   5948 H  HB3  . SER   B 1 128 ? 38.885 -28.643 4.733   1.00 17.26 ?  128 SER   B HB3  1 
ATOM   5949 H  HG   . SER   B 1 128 ? 39.175 -26.503 5.165   1.00 17.85 ?  128 SER   B HG   1 
ATOM   5950 N  N    . ALA   B 1 129 ? 41.388 -29.606 1.902   1.00 16.68 ?  129 ALA   B N    1 
ATOM   5951 C  CA   . ALA   B 1 129 ? 41.936 -30.906 1.544   1.00 17.16 ?  129 ALA   B CA   1 
ATOM   5952 C  C    . ALA   B 1 129 ? 43.332 -31.080 2.133   1.00 16.13 ?  129 ALA   B C    1 
ATOM   5953 O  O    . ALA   B 1 129 ? 43.896 -30.177 2.765   1.00 15.95 ?  129 ALA   B O    1 
ATOM   5954 C  CB   . ALA   B 1 129 ? 41.983 -31.059 0.026   1.00 19.41 ?  129 ALA   B CB   1 
ATOM   5955 H  H    . ALA   B 1 129 ? 41.475 -29.012 1.282   1.00 20.00 ?  129 ALA   B H    1 
ATOM   5956 H  HA   . ALA   B 1 129 ? 41.364 -31.601 1.900   1.00 20.58 ?  129 ALA   B HA   1 
ATOM   5957 H  HB1  . ALA   B 1 129 ? 42.342 -31.934 -0.191  1.00 23.27 ?  129 ALA   B HB1  1 
ATOM   5958 H  HB2  . ALA   B 1 129 ? 41.086 -30.971 -0.328  1.00 23.27 ?  129 ALA   B HB2  1 
ATOM   5959 H  HB3  . ALA   B 1 129 ? 42.556 -30.367 -0.344  1.00 23.27 ?  129 ALA   B HB3  1 
ATOM   5960 N  N    . GLY   B 1 130 ? 43.899 -32.265 1.904   1.00 16.03 ?  130 GLY   B N    1 
ATOM   5961 C  CA   . GLY   B 1 130 ? 45.287 -32.497 2.258   1.00 16.65 ?  130 GLY   B CA   1 
ATOM   5962 C  C    . GLY   B 1 130 ? 45.498 -32.410 3.751   1.00 16.70 ?  130 GLY   B C    1 
ATOM   5963 O  O    . GLY   B 1 130 ? 44.795 -33.054 4.543   1.00 17.55 ?  130 GLY   B O    1 
ATOM   5964 H  H    . GLY   B 1 130 ? 43.505 -32.936 1.540   1.00 19.22 ?  130 GLY   B H    1 
ATOM   5965 H  HA2  . GLY   B 1 130 ? 45.557 -33.378 1.960   1.00 19.96 ?  130 GLY   B HA2  1 
ATOM   5966 H  HA3  . GLY   B 1 130 ? 45.851 -31.836 1.826   1.00 19.96 ?  130 GLY   B HA3  1 
ATOM   5967 N  N    . ILE   B 1 131 ? 46.477 -31.586 4.141   1.00 17.02 ?  131 ILE   B N    1 
ATOM   5968 C  CA   . ILE   B 1 131 ? 46.840 -31.450 5.544   1.00 18.00 ?  131 ILE   B CA   1 
ATOM   5969 C  C    . ILE   B 1 131 ? 45.723 -30.846 6.378   1.00 17.16 ?  131 ILE   B C    1 
ATOM   5970 O  O    . ILE   B 1 131 ? 45.792 -30.914 7.608   1.00 18.63 ?  131 ILE   B O    1 
ATOM   5971 C  CB   . ILE   B 1 131 ? 48.164 -30.671 5.720   1.00 19.80 ?  131 ILE   B CB   1 
ATOM   5972 C  CG1  . ILE   B 1 131 ? 47.989 -29.190 5.358   1.00 20.83 ?  131 ILE   B CG1  1 
ATOM   5973 C  CG2  . ILE   B 1 131 ? 49.272 -31.304 4.878   1.00 21.19 ?  131 ILE   B CG2  1 
ATOM   5974 C  CD1  . ILE   B 1 131 ? 49.198 -28.323 5.669   1.00 21.92 ?  131 ILE   B CD1  1 
ATOM   5975 H  H    . ILE   B 1 131 ? 46.942 -31.091 3.617   1.00 20.40 ?  131 ILE   B H    1 
ATOM   5976 H  HA   . ILE   B 1 131 ? 46.993 -32.337 5.897   1.00 21.58 ?  131 ILE   B HA   1 
ATOM   5977 H  HB   . ILE   B 1 131 ? 48.426 -30.724 6.652   1.00 23.74 ?  131 ILE   B HB   1 
ATOM   5978 H  HG12 . ILE   B 1 131 ? 47.809 -29.124 4.409   1.00 24.98 ?  131 ILE   B HG12 1 
ATOM   5979 H  HG13 . ILE   B 1 131 ? 47.239 -28.828 5.858   1.00 24.98 ?  131 ILE   B HG13 1 
ATOM   5980 H  HG21 . ILE   B 1 131 ? 50.119 -30.901 5.118   1.00 25.41 ?  131 ILE   B HG21 1 
ATOM   5981 H  HG22 . ILE   B 1 131 ? 49.292 -32.255 5.055   1.00 25.41 ?  131 ILE   B HG22 1 
ATOM   5982 H  HG23 . ILE   B 1 131 ? 49.081 -31.145 3.940   1.00 25.41 ?  131 ILE   B HG23 1 
ATOM   5983 H  HD11 . ILE   B 1 131 ? 48.971 -27.397 5.490   1.00 26.29 ?  131 ILE   B HD11 1 
ATOM   5984 H  HD12 . ILE   B 1 131 ? 49.431 -28.433 6.604   1.00 26.29 ?  131 ILE   B HD12 1 
ATOM   5985 H  HD13 . ILE   B 1 131 ? 49.935 -28.600 5.107   1.00 26.29 ?  131 ILE   B HD13 1 
ATOM   5986 N  N    . PHE   B 1 132 ? 44.695 -30.264 5.745   1.00 16.21 ?  132 PHE   B N    1 
ATOM   5987 C  CA   . PHE   B 1 132 ? 43.532 -29.758 6.469   1.00 16.64 ?  132 PHE   B CA   1 
ATOM   5988 C  C    . PHE   B 1 132 ? 42.509 -30.846 6.801   1.00 18.11 ?  132 PHE   B C    1 
ATOM   5989 O  O    . PHE   B 1 132 ? 41.601 -30.589 7.599   1.00 19.70 ?  132 PHE   B O    1 
ATOM   5990 C  CB   . PHE   B 1 132 ? 42.849 -28.633 5.682   1.00 15.56 ?  132 PHE   B CB   1 
ATOM   5991 C  CG   . PHE   B 1 132 ? 43.542 -27.290 5.783   1.00 15.44 ?  132 PHE   B CG   1 
ATOM   5992 C  CD1  . PHE   B 1 132 ? 44.830 -27.108 5.298   1.00 16.17 ?  132 PHE   B CD1  1 
ATOM   5993 C  CD2  . PHE   B 1 132 ? 42.876 -26.192 6.316   1.00 15.13 ?  132 PHE   B CD2  1 
ATOM   5994 C  CE1  . PHE   B 1 132 ? 45.450 -25.866 5.382   1.00 16.78 ?  132 PHE   B CE1  1 
ATOM   5995 C  CE2  . PHE   B 1 132 ? 43.486 -24.948 6.393   1.00 15.66 ?  132 PHE   B CE2  1 
ATOM   5996 C  CZ   . PHE   B 1 132 ? 44.771 -24.789 5.929   1.00 16.46 ?  132 PHE   B CZ   1 
ATOM   5997 H  H    . PHE   B 1 132 ? 44.652 -30.153 4.894   1.00 19.44 ?  132 PHE   B H    1 
ATOM   5998 H  HA   . PHE   B 1 132 ? 43.837 -29.380 7.305   1.00 19.95 ?  132 PHE   B HA   1 
ATOM   5999 H  HB2  . PHE   B 1 132 ? 42.833 -28.880 4.746   1.00 18.66 ?  132 PHE   B HB2  1 
ATOM   6000 H  HB3  . PHE   B 1 132 ? 41.945 -28.526 6.013   1.00 18.66 ?  132 PHE   B HB3  1 
ATOM   6001 H  HD1  . PHE   B 1 132 ? 45.292 -27.830 4.935   1.00 19.39 ?  132 PHE   B HD1  1 
ATOM   6002 H  HD2  . PHE   B 1 132 ? 42.009 -26.299 6.636   1.00 18.14 ?  132 PHE   B HD2  1 
ATOM   6003 H  HE1  . PHE   B 1 132 ? 46.317 -25.757 5.066   1.00 20.12 ?  132 PHE   B HE1  1 
ATOM   6004 H  HE2  . PHE   B 1 132 ? 43.030 -24.228 6.768   1.00 18.78 ?  132 PHE   B HE2  1 
ATOM   6005 H  HZ   . PHE   B 1 132 ? 45.184 -23.954 5.987   1.00 19.73 ?  132 PHE   B HZ   1 
ATOM   6006 N  N    . GLY   B 1 133 ? 42.608 -32.041 6.204   1.00 17.65 ?  133 GLY   B N    1 
ATOM   6007 C  CA   . GLY   B 1 133 ? 41.894 -33.205 6.701   1.00 18.51 ?  133 GLY   B CA   1 
ATOM   6008 C  C    . GLY   B 1 133 ? 40.502 -33.475 6.156   1.00 18.98 ?  133 GLY   B C    1 
ATOM   6009 O  O    . GLY   B 1 133 ? 39.922 -34.508 6.509   1.00 20.77 ?  133 GLY   B O    1 
ATOM   6010 H  H    . GLY   B 1 133 ? 43.093 -32.198 5.508   1.00 21.16 ?  133 GLY   B H    1 
ATOM   6011 H  HA2  . GLY   B 1 133 ? 42.432 -33.990 6.522   1.00 22.20 ?  133 GLY   B HA2  1 
ATOM   6012 H  HA3  . GLY   B 1 133 ? 41.814 -33.119 7.664   1.00 22.20 ?  133 GLY   B HA3  1 
ATOM   6013 N  N    . ALA   B 1 134 ? 39.935 -32.601 5.331   1.00 17.82 ?  134 ALA   B N    1 
ATOM   6014 C  CA   . ALA   B 1 134 ? 38.611 -32.886 4.799   1.00 17.71 ?  134 ALA   B CA   1 
ATOM   6015 C  C    . ALA   B 1 134 ? 38.695 -33.876 3.643   1.00 17.92 ?  134 ALA   B C    1 
ATOM   6016 O  O    . ALA   B 1 134 ? 39.747 -34.068 3.026   1.00 18.81 ?  134 ALA   B O    1 
ATOM   6017 C  CB   . ALA   B 1 134 ? 37.928 -31.602 4.329   1.00 18.14 ?  134 ALA   B CB   1 
ATOM   6018 H  H    . ALA   B 1 134 ? 40.283 -31.850 5.076   1.00 21.37 ?  134 ALA   B H    1 
ATOM   6019 H  HA   . ALA   B 1 134 ? 38.065 -33.274 5.501   1.00 21.24 ?  134 ALA   B HA   1 
ATOM   6020 H  HB1  . ALA   B 1 134 ? 37.039 -31.820 4.003   1.00 21.75 ?  134 ALA   B HB1  1 
ATOM   6021 H  HB2  . ALA   B 1 134 ? 37.862 -30.984 5.075   1.00 21.75 ?  134 ALA   B HB2  1 
ATOM   6022 H  HB3  . ALA   B 1 134 ? 38.452 -31.206 3.617   1.00 21.75 ?  134 ALA   B HB3  1 
ATOM   6023 N  N    . ASP   B 1 135 ? 37.560 -34.501 3.354   1.00 18.34 ?  135 ASP   B N    1 
ATOM   6024 C  CA   . ASP   B 1 135 ? 37.456 -35.393 2.210   1.00 18.91 ?  135 ASP   B CA   1 
ATOM   6025 C  C    . ASP   B 1 135 ? 37.553 -34.559 0.939   1.00 17.46 ?  135 ASP   B C    1 
ATOM   6026 O  O    . ASP   B 1 135 ? 36.697 -33.688 0.713   1.00 17.44 ?  135 ASP   B O    1 
ATOM   6027 C  CB   . ASP   B 1 135 ? 36.114 -36.117 2.268   1.00 20.99 ?  135 ASP   B CB   1 
ATOM   6028 C  CG   . ASP   B 1 135 ? 35.935 -37.119 1.150   1.00 23.19 ?  135 ASP   B CG   1 
ATOM   6029 O  OD1  . ASP   B 1 135 ? 36.794 -37.174 0.245   1.00 22.88 ?  135 ASP   B OD1  1 
ATOM   6030 O  OD2  . ASP   B 1 135 ? 34.939 -37.880 1.191   1.00 25.92 -1 135 ASP   B OD2  1 
ATOM   6031 H  H    . ASP   B 1 135 ? 36.833 -34.424 3.809   1.00 22.00 ?  135 ASP   B H    1 
ATOM   6032 H  HA   . ASP   B 1 135 ? 38.172 -36.049 2.242   1.00 22.68 ?  135 ASP   B HA   1 
ATOM   6033 H  HB2  . ASP   B 1 135 ? 36.052 -36.594 3.108   1.00 25.18 ?  135 ASP   B HB2  1 
ATOM   6034 H  HB3  . ASP   B 1 135 ? 35.405 -35.464 2.198   1.00 25.18 ?  135 ASP   B HB3  1 
ATOM   6035 N  N    . PRO   B 1 136 ? 38.566 -34.764 0.095   1.00 17.65 ?  136 PRO   B N    1 
ATOM   6036 C  CA   . PRO   B 1 136 ? 38.665 -33.945 -1.123  1.00 16.79 ?  136 PRO   B CA   1 
ATOM   6037 C  C    . PRO   B 1 136 ? 37.475 -34.097 -2.049  1.00 16.43 ?  136 PRO   B C    1 
ATOM   6038 O  O    . PRO   B 1 136 ? 37.159 -33.153 -2.780  1.00 15.69 ?  136 PRO   B O    1 
ATOM   6039 C  CB   . PRO   B 1 136 ? 39.975 -34.421 -1.767  1.00 17.76 ?  136 PRO   B CB   1 
ATOM   6040 C  CG   . PRO   B 1 136 ? 40.187 -35.809 -1.216  1.00 19.03 ?  136 PRO   B CG   1 
ATOM   6041 C  CD   . PRO   B 1 136 ? 39.651 -35.758 0.185   1.00 18.75 ?  136 PRO   B CD   1 
ATOM   6042 H  HA   . PRO   B 1 136 ? 38.754 -33.011 -0.887  1.00 20.14 ?  136 PRO   B HA   1 
ATOM   6043 H  HB2  . PRO   B 1 136 ? 39.881 -34.445 -2.734  1.00 21.30 ?  136 PRO   B HB2  1 
ATOM   6044 H  HB3  . PRO   B 1 136 ? 40.701 -33.832 -1.508  1.00 21.30 ?  136 PRO   B HB3  1 
ATOM   6045 H  HG2  . PRO   B 1 136 ? 39.692 -36.454 -1.747  1.00 22.82 ?  136 PRO   B HG2  1 
ATOM   6046 H  HG3  . PRO   B 1 136 ? 41.134 -36.022 -1.213  1.00 22.82 ?  136 PRO   B HG3  1 
ATOM   6047 H  HD2  . PRO   B 1 136 ? 39.302 -36.623 0.447   1.00 22.48 ?  136 PRO   B HD2  1 
ATOM   6048 H  HD3  . PRO   B 1 136 ? 40.337 -35.449 0.803   1.00 22.48 ?  136 PRO   B HD3  1 
ATOM   6049 N  N    . ILE   B 1 137 ? 36.812 -35.260 -2.046  1.00 16.94 ?  137 ILE   B N    1 
ATOM   6050 C  CA   . ILE   B 1 137 ? 35.595 -35.430 -2.836  1.00 17.16 ?  137 ILE   B CA   1 
ATOM   6051 C  C    . ILE   B 1 137 ? 34.521 -34.461 -2.358  1.00 16.61 ?  137 ILE   B C    1 
ATOM   6052 O  O    . ILE   B 1 137 ? 33.807 -33.847 -3.162  1.00 16.10 ?  137 ILE   B O    1 
ATOM   6053 C  CB   . ILE   B 1 137 ? 35.123 -36.898 -2.776  1.00 19.49 ?  137 ILE   B CB   1 
ATOM   6054 C  CG1  . ILE   B 1 137 ? 36.128 -37.802 -3.498  1.00 21.84 ?  137 ILE   B CG1  1 
ATOM   6055 C  CG2  . ILE   B 1 137 ? 33.718 -37.041 -3.362  1.00 19.85 ?  137 ILE   B CG2  1 
ATOM   6056 C  CD1  . ILE   B 1 137 ? 35.841 -39.286 -3.352  1.00 24.29 ?  137 ILE   B CD1  1 
ATOM   6057 H  H    . ILE   B 1 137 ? 37.044 -35.958 -1.601  1.00 20.31 ?  137 ILE   B H    1 
ATOM   6058 H  HA   . ILE   B 1 137 ? 35.789 -35.222 -3.765  1.00 20.58 ?  137 ILE   B HA   1 
ATOM   6059 H  HB   . ILE   B 1 137 ? 35.087 -37.166 -1.849  1.00 23.38 ?  137 ILE   B HB   1 
ATOM   6060 H  HG12 . ILE   B 1 137 ? 36.117 -37.595 -4.445  1.00 26.19 ?  137 ILE   B HG12 1 
ATOM   6061 H  HG13 . ILE   B 1 137 ? 37.011 -37.639 -3.135  1.00 26.19 ?  137 ILE   B HG13 1 
ATOM   6062 H  HG21 . ILE   B 1 137 ? 33.506 -37.983 -3.473  1.00 23.81 ?  137 ILE   B HG21 1 
ATOM   6063 H  HG22 . ILE   B 1 137 ? 33.074 -36.640 -2.756  1.00 23.81 ?  137 ILE   B HG22 1 
ATOM   6064 H  HG23 . ILE   B 1 137 ? 33.682 -36.596 -4.223  1.00 23.81 ?  137 ILE   B HG23 1 
ATOM   6065 H  HD11 . ILE   B 1 137 ? 36.581 -39.782 -3.734  1.00 29.13 ?  137 ILE   B HD11 1 
ATOM   6066 H  HD12 . ILE   B 1 137 ? 35.749 -39.502 -2.410  1.00 29.13 ?  137 ILE   B HD12 1 
ATOM   6067 H  HD13 . ILE   B 1 137 ? 35.023 -39.505 -3.825  1.00 29.13 ?  137 ILE   B HD13 1 
ATOM   6068 N  N    . HIS   B 1 138 ? 34.392 -34.310 -1.042  1.00 16.78 ?  138 HIS   B N    1 
ATOM   6069 C  CA   . HIS   B 1 138 ? 33.445 -33.343 -0.502  1.00 17.12 ?  138 HIS   B CA   1 
ATOM   6070 C  C    . HIS   B 1 138 ? 33.863 -31.916 -0.831  1.00 16.24 ?  138 HIS   B C    1 
ATOM   6071 O  O    . HIS   B 1 138 ? 33.016 -31.070 -1.139  1.00 16.78 ?  138 HIS   B O    1 
ATOM   6072 C  CB   . HIS   B 1 138 ? 33.336 -33.513 1.007   1.00 18.54 ?  138 HIS   B CB   1 
ATOM   6073 C  CG   . HIS   B 1 138 ? 32.406 -32.533 1.642   1.00 19.78 ?  138 HIS   B CG   1 
ATOM   6074 N  ND1  . HIS   B 1 138 ? 31.069 -32.460 1.314   1.00 21.15 ?  138 HIS   B ND1  1 
ATOM   6075 C  CD2  . HIS   B 1 138 ? 32.625 -31.556 2.553   1.00 20.45 ?  138 HIS   B CD2  1 
ATOM   6076 C  CE1  . HIS   B 1 138 ? 30.499 -31.494 2.012   1.00 21.33 ?  138 HIS   B CE1  1 
ATOM   6077 N  NE2  . HIS   B 1 138 ? 31.422 -30.931 2.773   1.00 20.69 ?  138 HIS   B NE2  1 
ATOM   6078 H  H    . HIS   B 1 138 ? 34.834 -34.756 -0.453  1.00 20.12 ?  138 HIS   B H    1 
ATOM   6079 H  HA   . HIS   B 1 138 ? 32.570 -33.509 -0.889  1.00 20.52 ?  138 HIS   B HA   1 
ATOM   6080 H  HB2  . HIS   B 1 138 ? 33.004 -34.404 1.203   1.00 22.23 ?  138 HIS   B HB2  1 
ATOM   6081 H  HB3  . HIS   B 1 138 ? 34.211 -33.391 1.402   1.00 22.23 ?  138 HIS   B HB3  1 
ATOM   6082 H  HD1  . HIS   B 1 138 ? 30.666 -32.970 0.748   1.00 25.36 ?  138 HIS   B HD1  1 
ATOM   6083 H  HD2  . HIS   B 1 138 ? 33.427 -31.355 2.968   1.00 24.53 ?  138 HIS   B HD2  1 
ATOM   6084 H  HE1  . HIS   B 1 138 ? 29.596 -31.258 1.977   1.00 25.58 ?  138 HIS   B HE1  1 
ATOM   6085 N  N    . SER   B 1 139 ? 35.159 -31.617 -0.757  1.00 15.86 ?  139 SER   B N    1 
ATOM   6086 C  CA   . SER   B 1 139 ? 35.593 -30.266 -1.078  1.00 15.19 ?  139 SER   B CA   1 
ATOM   6087 C  C    . SER   B 1 139 ? 35.261 -29.920 -2.519  1.00 14.12 ?  139 SER   B C    1 
ATOM   6088 O  O    . SER   B 1 139 ? 34.816 -28.805 -2.804  1.00 14.22 ?  139 SER   B O    1 
ATOM   6089 C  CB   . SER   B 1 139 ? 37.084 -30.119 -0.803  1.00 15.61 ?  139 SER   B CB   1 
ATOM   6090 O  OG   . SER   B 1 139 ? 37.496 -28.792 -1.077  1.00 15.52 ?  139 SER   B OG   1 
ATOM   6091 H  H    . SER   B 1 139 ? 35.779 -32.163 -0.536  1.00 19.02 ?  139 SER   B H    1 
ATOM   6092 H  HA   . SER   B 1 139 ? 35.115 -29.643 -0.512  1.00 18.21 ?  139 SER   B HA   1 
ATOM   6093 H  HB2  . SER   B 1 139 ? 37.253 -30.321 0.131   1.00 18.71 ?  139 SER   B HB2  1 
ATOM   6094 H  HB3  . SER   B 1 139 ? 37.576 -30.730 -1.371  1.00 18.71 ?  139 SER   B HB3  1 
ATOM   6095 H  HG   . SER   B 1 139 ? 38.321 -28.710 -0.919  1.00 18.61 ?  139 SER   B HG   1 
ATOM   6096 N  N    . LEU   B 1 140 ? 35.450 -30.864 -3.441  1.00 14.01 ?  140 LEU   B N    1 
ATOM   6097 C  CA   . LEU   B 1 140 ? 35.087 -30.617 -4.830  1.00 14.28 ?  140 LEU   B CA   1 
ATOM   6098 C  C    . LEU   B 1 140 ? 33.586 -30.386 -4.968  1.00 14.37 ?  140 LEU   B C    1 
ATOM   6099 O  O    . LEU   B 1 140 ? 33.151 -29.502 -5.712  1.00 14.44 ?  140 LEU   B O    1 
ATOM   6100 C  CB   . LEU   B 1 140 ? 35.561 -31.780 -5.704  1.00 14.42 ?  140 LEU   B CB   1 
ATOM   6101 C  CG   . LEU   B 1 140 ? 35.195 -31.678 -7.178  1.00 14.74 ?  140 LEU   B CG   1 
ATOM   6102 C  CD1  . LEU   B 1 140 ? 35.748 -30.396 -7.774  1.00 15.51 ?  140 LEU   B CD1  1 
ATOM   6103 C  CD2  . LEU   B 1 140 ? 35.684 -32.900 -7.928  1.00 15.64 ?  140 LEU   B CD2  1 
ATOM   6104 H  H    . LEU   B 1 140 ? 35.782 -31.642 -3.291  1.00 16.79 ?  140 LEU   B H    1 
ATOM   6105 H  HA   . LEU   B 1 140 ? 35.545 -29.817 -5.136  1.00 17.12 ?  140 LEU   B HA   1 
ATOM   6106 H  HB2  . LEU   B 1 140 ? 36.530 -31.840 -5.650  1.00 17.29 ?  140 LEU   B HB2  1 
ATOM   6107 H  HB3  . LEU   B 1 140 ? 35.169 -32.602 -5.368  1.00 17.29 ?  140 LEU   B HB3  1 
ATOM   6108 H  HG   . LEU   B 1 140 ? 34.231 -31.643 -7.259  1.00 17.68 ?  140 LEU   B HG   1 
ATOM   6109 H  HD11 . LEU   B 1 140 ? 35.639 -30.426 -8.736  1.00 18.59 ?  140 LEU   B HD11 1 
ATOM   6110 H  HD12 . LEU   B 1 140 ? 35.257 -29.640 -7.410  1.00 18.59 ?  140 LEU   B HD12 1 
ATOM   6111 H  HD13 . LEU   B 1 140 ? 36.687 -30.321 -7.547  1.00 18.59 ?  140 LEU   B HD13 1 
ATOM   6112 H  HD21 . LEU   B 1 140 ? 35.436 -32.808 -8.862  1.00 18.76 ?  140 LEU   B HD21 1 
ATOM   6113 H  HD22 . LEU   B 1 140 ? 36.643 -32.959 -7.840  1.00 18.76 ?  140 LEU   B HD22 1 
ATOM   6114 H  HD23 . LEU   B 1 140 ? 35.260 -33.683 -7.548  1.00 18.76 ?  140 LEU   B HD23 1 
ATOM   6115 N  N    . ARG   B 1 141 ? 32.785 -31.182 -4.258  1.00 14.63 ?  141 ARG   B N    1 
ATOM   6116 C  CA   . ARG   B 1 141 ? 31.337 -31.001 -4.238  1.00 15.40 ?  141 ARG   B CA   1 
ATOM   6117 C  C    . ARG   B 1 141 ? 30.962 -29.588 -3.812  1.00 14.83 ?  141 ARG   B C    1 
ATOM   6118 O  O    . ARG   B 1 141 ? 30.156 -28.913 -4.471  1.00 15.39 ?  141 ARG   B O    1 
ATOM   6119 C  CB   . ARG   B 1 141 ? 30.750 -32.028 -3.261  1.00 16.87 ?  141 ARG   B CB   1 
ATOM   6120 C  CG   . ARG   B 1 141 ? 29.279 -31.911 -2.943  1.00 18.43 ?  141 ARG   B CG   1 
ATOM   6121 C  CD   . ARG   B 1 141 ? 28.482 -32.556 -4.006  1.00 20.14 ?  141 ARG   B CD   1 
ATOM   6122 N  NE   . ARG   B 1 141 ? 28.215 -31.652 -5.113  1.00 20.63 ?  141 ARG   B NE   1 
ATOM   6123 C  CZ   . ARG   B 1 141 ? 28.219 -32.005 -6.390  1.00 20.19 ?  141 ARG   B CZ   1 
ATOM   6124 N  NH1  . ARG   B 1 141 ? 28.651 -33.193 -6.780  1.00 19.96 ?  141 ARG   B NH1  1 
ATOM   6125 N  NH2  . ARG   B 1 141 ? 27.778 -31.142 -7.300  1.00 21.00 ?  141 ARG   B NH2  1 
ATOM   6126 H  H    . ARG   B 1 141 ? 33.064 -31.836 -3.778  1.00 17.54 ?  141 ARG   B H    1 
ATOM   6127 H  HA   . ARG   B 1 141 ? 30.974 -31.163 -5.119  1.00 18.47 ?  141 ARG   B HA   1 
ATOM   6128 H  HB2  . ARG   B 1 141 ? 30.906 -32.914 -3.628  1.00 20.23 ?  141 ARG   B HB2  1 
ATOM   6129 H  HB3  . ARG   B 1 141 ? 31.230 -31.951 -2.422  1.00 20.23 ?  141 ARG   B HB3  1 
ATOM   6130 H  HG2  . ARG   B 1 141 ? 29.102 -32.352 -2.102  1.00 22.10 ?  141 ARG   B HG2  1 
ATOM   6131 H  HG3  . ARG   B 1 141 ? 29.025 -30.971 -2.888  1.00 22.10 ?  141 ARG   B HG3  1 
ATOM   6132 H  HD2  . ARG   B 1 141 ? 28.966 -33.332 -4.339  1.00 24.15 ?  141 ARG   B HD2  1 
ATOM   6133 H  HD3  . ARG   B 1 141 ? 27.637 -32.839 -3.634  1.00 24.15 ?  141 ARG   B HD3  1 
ATOM   6134 H  HE   . ARG   B 1 141 ? 28.027 -30.835 -4.922  1.00 24.74 ?  141 ARG   B HE   1 
ATOM   6135 H  HH11 . ARG   B 1 141 ? 28.931 -33.769 -6.205  1.00 23.93 ?  141 ARG   B HH11 1 
ATOM   6136 H  HH12 . ARG   B 1 141 ? 28.652 -33.395 -7.614  1.00 23.93 ?  141 ARG   B HH12 1 
ATOM   6137 H  HH21 . ARG   B 1 141 ? 27.504 -30.362 -7.058  1.00 25.18 ?  141 ARG   B HH21 1 
ATOM   6138 H  HH22 . ARG   B 1 141 ? 27.794 -31.350 -8.135  1.00 25.18 ?  141 ARG   B HH22 1 
ATOM   6139 N  N    . VAL   B 1 142 ? 31.502 -29.141 -2.682  1.00 14.46 ?  142 VAL   B N    1 
ATOM   6140 C  CA   . VAL   B 1 142 ? 31.165 -27.808 -2.198  1.00 14.33 ?  142 VAL   B CA   1 
ATOM   6141 C  C    . VAL   B 1 142 ? 31.641 -26.752 -3.188  1.00 14.30 ?  142 VAL   B C    1 
ATOM   6142 O  O    . VAL   B 1 142 ? 30.943 -25.763 -3.446  1.00 14.81 ?  142 VAL   B O    1 
ATOM   6143 C  CB   . VAL   B 1 142 ? 31.713 -27.580 -0.777  1.00 15.07 ?  142 VAL   B CB   1 
ATOM   6144 C  CG1  . VAL   B 1 142 ? 31.409 -26.155 -0.310  1.00 15.10 ?  142 VAL   B CG1  1 
ATOM   6145 C  CG2  . VAL   B 1 142 ? 31.121 -28.599 0.184   1.00 15.66 ?  142 VAL   B CG2  1 
ATOM   6146 H  H    . VAL   B 1 142 ? 32.062 -29.576 -2.188  1.00 17.34 ?  142 VAL   B H    1 
ATOM   6147 H  HA   . VAL   B 1 142 ? 30.205 -27.741 -2.145  1.00 17.17 ?  142 VAL   B HA   1 
ATOM   6148 H  HB   . VAL   B 1 142 ? 32.678 -27.697 -0.782  1.00 18.07 ?  142 VAL   B HB   1 
ATOM   6149 H  HG11 . VAL   B 1 142 ? 31.594 -26.090 0.638   1.00 18.10 ?  142 VAL   B HG11 1 
ATOM   6150 H  HG12 . VAL   B 1 142 ? 31.975 -25.535 -0.799  1.00 18.10 ?  142 VAL   B HG12 1 
ATOM   6151 H  HG13 . VAL   B 1 142 ? 30.477 -25.961 -0.482  1.00 18.10 ?  142 VAL   B HG13 1 
ATOM   6152 H  HG21 . VAL   B 1 142 ? 31.439 -28.412 1.080   1.00 18.77 ?  142 VAL   B HG21 1 
ATOM   6153 H  HG22 . VAL   B 1 142 ? 30.154 -28.534 0.154   1.00 18.77 ?  142 VAL   B HG22 1 
ATOM   6154 H  HG23 . VAL   B 1 142 ? 31.400 -29.489 -0.087  1.00 18.77 ?  142 VAL   B HG23 1 
ATOM   6155 N  N    . CYS   B 1 143 ? 32.827 -26.945 -3.764  1.00 14.00 ?  143 CYS   B N    1 
ATOM   6156 C  CA   . CYS   B 1 143 ? 33.322 -26.013 -4.772  1.00 14.01 ?  143 CYS   B CA   1 
ATOM   6157 C  C    . CYS   B 1 143 ? 32.320 -25.870 -5.911  1.00 13.76 ?  143 CYS   B C    1 
ATOM   6158 O  O    . CYS   B 1 143 ? 31.923 -24.758 -6.276  1.00 13.94 ?  143 CYS   B O    1 
ATOM   6159 C  CB   . CYS   B 1 143 ? 34.679 -26.497 -5.298  1.00 14.10 ?  143 CYS   B CB   1 
ATOM   6160 S  SG   . CYS   B 1 143 ? 35.425 -25.398 -6.527  1.00 14.56 ?  143 CYS   B SG   1 
ATOM   6161 H  H    . CYS   B 1 143 ? 33.362 -27.592 -3.587  1.00 16.79 ?  143 CYS   B H    1 
ATOM   6162 H  HA   . CYS   B 1 143 ? 33.454 -25.138 -4.372  1.00 16.79 ?  143 CYS   B HA   1 
ATOM   6163 H  HB2  . CYS   B 1 143 ? 35.304 -26.571 -4.557  1.00 16.91 ?  143 CYS   B HB2  1 
ATOM   6164 H  HB3  . CYS   B 1 143 ? 34.566 -27.366 -5.710  1.00 16.91 ?  143 CYS   B HB3  1 
ATOM   6165 H  HG   . CYS   B 1 143 ? 36.505 -25.830 -6.840  1.00 17.45 ?  143 CYS   B HG   1 
ATOM   6166 N  N    . VAL   B 1 144 ? 31.913 -26.991 -6.500  1.00 14.09 ?  144 VAL   B N    1 
ATOM   6167 C  CA   . VAL   B 1 144 ? 31.006 -26.941 -7.642  1.00 15.10 ?  144 VAL   B CA   1 
ATOM   6168 C  C    . VAL   B 1 144 ? 29.669 -26.319 -7.263  1.00 15.32 ?  144 VAL   B C    1 
ATOM   6169 O  O    . VAL   B 1 144 ? 29.052 -25.613 -8.070  1.00 16.34 ?  144 VAL   B O    1 
ATOM   6170 C  CB   . VAL   B 1 144 ? 30.837 -28.353 -8.216  1.00 17.66 ?  144 VAL   B CB   1 
ATOM   6171 C  CG1  . VAL   B 1 144 ? 29.559 -28.471 -9.047  1.00 20.15 ?  144 VAL   B CG1  1 
ATOM   6172 C  CG2  . VAL   B 1 144 ? 32.079 -28.747 -9.011  1.00 17.99 ?  144 VAL   B CG2  1 
ATOM   6173 H  H    . VAL   B 1 144 ? 32.152 -27.786 -6.272  1.00 16.90 ?  144 VAL   B H    1 
ATOM   6174 H  HA   . VAL   B 1 144 ? 31.392 -26.383 -8.333  1.00 18.10 ?  144 VAL   B HA   1 
ATOM   6175 H  HB   . VAL   B 1 144 ? 30.760 -28.976 -7.476  1.00 21.18 ?  144 VAL   B HB   1 
ATOM   6176 H  HG11 . VAL   B 1 144 ? 29.629 -29.260 -9.610  1.00 24.16 ?  144 VAL   B HG11 1 
ATOM   6177 H  HG12 . VAL   B 1 144 ? 28.801 -28.563 -8.450  1.00 24.16 ?  144 VAL   B HG12 1 
ATOM   6178 H  HG13 . VAL   B 1 144 ? 29.464 -27.682 -9.598  1.00 24.16 ?  144 VAL   B HG13 1 
ATOM   6179 H  HG21 . VAL   B 1 144 ? 31.959 -29.643 -9.360  1.00 21.57 ?  144 VAL   B HG21 1 
ATOM   6180 H  HG22 . VAL   B 1 144 ? 32.194 -28.119 -9.744  1.00 21.57 ?  144 VAL   B HG22 1 
ATOM   6181 H  HG23 . VAL   B 1 144 ? 32.850 -28.716 -8.426  1.00 21.57 ?  144 VAL   B HG23 1 
ATOM   6182 N  N    . ASP   B 1 145 ? 29.201 -26.566 -6.044  1.00 15.66 ?  145 ASP   B N    1 
ATOM   6183 C  CA   . ASP   B 1 145 ? 27.891 -26.095 -5.615  1.00 16.48 ?  145 ASP   B CA   1 
ATOM   6184 C  C    . ASP   B 1 145 ? 27.920 -24.670 -5.077  1.00 15.91 ?  145 ASP   B C    1 
ATOM   6185 O  O    . ASP   B 1 145 ? 26.858 -24.128 -4.745  1.00 17.67 ?  145 ASP   B O    1 
ATOM   6186 C  CB   . ASP   B 1 145 ? 27.303 -27.014 -4.534  1.00 17.93 ?  145 ASP   B CB   1 
ATOM   6187 C  CG   . ASP   B 1 145 ? 26.940 -28.387 -5.047  1.00 19.75 ?  145 ASP   B CG   1 
ATOM   6188 O  OD1  . ASP   B 1 145 ? 26.837 -28.578 -6.275  1.00 20.09 ?  145 ASP   B OD1  1 
ATOM   6189 O  OD2  . ASP   B 1 145 ? 26.752 -29.273 -4.194  1.00 21.71 -1 145 ASP   B OD2  1 
ATOM   6190 H  H    . ASP   B 1 145 ? 29.634 -26.988 -5.435  1.00 18.78 ?  145 ASP   B H    1 
ATOM   6191 H  HA   . ASP   B 1 145 ? 27.295 -26.090 -6.375  1.00 19.76 ?  145 ASP   B HA   1 
ATOM   6192 H  HB2  . ASP   B 1 145 ? 27.953 -27.129 -3.833  1.00 21.50 ?  145 ASP   B HB2  1 
ATOM   6193 H  HB3  . ASP   B 1 145 ? 26.495 -26.604 -4.184  1.00 21.50 ?  145 ASP   B HB3  1 
ATOM   6194 N  N    . THR   B 1 146 ? 29.099 -24.054 -4.974  1.00 14.17 ?  146 THR   B N    1 
ATOM   6195 C  CA   . THR   B 1 146 ? 29.226 -22.730 -4.371  1.00 13.76 ?  146 THR   B CA   1 
ATOM   6196 C  C    . THR   B 1 146 ? 29.858 -21.700 -5.291  1.00 13.61 ?  146 THR   B C    1 
ATOM   6197 O  O    . THR   B 1 146 ? 29.403 -20.542 -5.338  1.00 13.78 ?  146 THR   B O    1 
ATOM   6198 C  CB   . THR   B 1 146 ? 30.056 -22.829 -3.085  1.00 13.82 ?  146 THR   B CB   1 
ATOM   6199 O  OG1  . THR   B 1 146 ? 29.480 -23.815 -2.221  1.00 14.14 ?  146 THR   B OG1  1 
ATOM   6200 C  CG2  . THR   B 1 146 ? 30.124 -21.492 -2.372  1.00 14.34 ?  146 THR   B CG2  1 
ATOM   6201 H  H    . THR   B 1 146 ? 29.852 -24.376 -5.248  1.00 16.99 ?  146 THR   B H    1 
ATOM   6202 H  HA   . THR   B 1 146 ? 28.352 -22.399 -4.131  1.00 16.50 ?  146 THR   B HA   1 
ATOM   6203 H  HB   . THR   B 1 146 ? 30.965 -23.084 -3.308  1.00 16.56 ?  146 THR   B HB   1 
ATOM   6204 H  HG1  . THR   B 1 146 ? 29.520 -24.577 -2.590  1.00 16.95 ?  146 THR   B HG1  1 
ATOM   6205 H  HG21 . THR   B 1 146 ? 30.465 -21.608 -1.473  1.00 17.19 ?  146 THR   B HG21 1 
ATOM   6206 H  HG22 . THR   B 1 146 ? 30.714 -20.885 -2.854  1.00 17.19 ?  146 THR   B HG22 1 
ATOM   6207 H  HG23 . THR   B 1 146 ? 29.240 -21.095 -2.325  1.00 17.19 ?  146 THR   B HG23 1 
ATOM   6208 N  N    . VAL   B 1 147 ? 30.923 -22.073 -5.993  1.00 13.49 ?  147 VAL   B N    1 
ATOM   6209 C  CA   . VAL   B 1 147 ? 31.648 -21.132 -6.833  1.00 13.36 ?  147 VAL   B CA   1 
ATOM   6210 C  C    . VAL   B 1 147 ? 30.916 -20.998 -8.155  1.00 13.37 ?  147 VAL   B C    1 
ATOM   6211 O  O    . VAL   B 1 147 ? 30.543 -22.002 -8.781  1.00 14.21 ?  147 VAL   B O    1 
ATOM   6212 C  CB   . VAL   B 1 147 ? 33.101 -21.590 -7.037  1.00 13.28 ?  147 VAL   B CB   1 
ATOM   6213 C  CG1  . VAL   B 1 147 ? 33.866 -20.559 -7.840  1.00 13.27 ?  147 VAL   B CG1  1 
ATOM   6214 C  CG2  . VAL   B 1 147 ? 33.779 -21.810 -5.698  1.00 13.20 ?  147 VAL   B CG2  1 
ATOM   6215 H  H    . VAL   B 1 147 ? 31.245 -22.876 -6.008  1.00 16.17 ?  147 VAL   B H    1 
ATOM   6216 H  HA   . VAL   B 1 147 ? 31.665 -20.265 -6.402  1.00 16.02 ?  147 VAL   B HA   1 
ATOM   6217 H  HB   . VAL   B 1 147 ? 33.111 -22.430 -7.529  1.00 15.92 ?  147 VAL   B HB   1 
ATOM   6218 H  HG11 . VAL   B 1 147 ? 34.807 -20.785 -7.835  1.00 15.91 ?  147 VAL   B HG11 1 
ATOM   6219 H  HG12 . VAL   B 1 147 ? 33.532 -20.550 -8.751  1.00 15.91 ?  147 VAL   B HG12 1 
ATOM   6220 H  HG13 . VAL   B 1 147 ? 33.734 -19.685 -7.433  1.00 15.91 ?  147 VAL   B HG13 1 
ATOM   6221 H  HG21 . VAL   B 1 147 ? 34.719 -22.006 -5.848  1.00 15.82 ?  147 VAL   B HG21 1 
ATOM   6222 H  HG22 . VAL   B 1 147 ? 33.693 -21.004 -5.166  1.00 15.82 ?  147 VAL   B HG22 1 
ATOM   6223 H  HG23 . VAL   B 1 147 ? 33.356 -22.554 -5.244  1.00 15.82 ?  147 VAL   B HG23 1 
ATOM   6224 N  N    . ARG   B 1 148 ? 30.707 -19.750 -8.578  1.00 13.33 ?  148 ARG   B N    1 
ATOM   6225 C  CA   . ARG   B 1 148 ? 30.084 -19.442 -9.853  1.00 13.40 ?  148 ARG   B CA   1 
ATOM   6226 C  C    . ARG   B 1 148 ? 31.041 -18.767 -10.825 1.00 13.40 ?  148 ARG   B C    1 
ATOM   6227 O  O    . ARG   B 1 148 ? 30.754 -18.738 -12.024 1.00 14.74 ?  148 ARG   B O    1 
ATOM   6228 C  CB   . ARG   B 1 148 ? 28.845 -18.554 -9.644  1.00 13.56 ?  148 ARG   B CB   1 
ATOM   6229 C  CG   . ARG   B 1 148 ? 27.768 -19.260 -8.831  1.00 14.42 ?  148 ARG   B CG   1 
ATOM   6230 C  CD   . ARG   B 1 148 ? 26.561 -18.369 -8.515  1.00 15.43 ?  148 ARG   B CD   1 
ATOM   6231 N  NE   . ARG   B 1 148 ? 26.949 -17.171 -7.780  1.00 15.15 ?  148 ARG   B NE   1 
ATOM   6232 C  CZ   . ARG   B 1 148 ? 27.245 -17.139 -6.488  1.00 14.25 ?  148 ARG   B CZ   1 
ATOM   6233 N  NH1  . ARG   B 1 148 ? 27.181 -18.226 -5.732  1.00 14.54 ?  148 ARG   B NH1  1 
ATOM   6234 N  NH2  . ARG   B 1 148 ? 27.639 -15.989 -5.944  1.00 14.35 ?  148 ARG   B NH2  1 
ATOM   6235 H  H    . ARG   B 1 148 ? 30.922 -19.048 -8.125  1.00 15.99 ?  148 ARG   B H    1 
ATOM   6236 H  HA   . ARG   B 1 148 ? 29.787 -20.266 -10.263 1.00 16.06 ?  148 ARG   B HA   1 
ATOM   6237 H  HB2  . ARG   B 1 148 ? 29.103 -17.752 -9.167  1.00 16.25 ?  148 ARG   B HB2  1 
ATOM   6238 H  HB3  . ARG   B 1 148 ? 28.468 -18.323 -10.508 1.00 16.25 ?  148 ARG   B HB3  1 
ATOM   6239 H  HG2  . ARG   B 1 148 ? 27.443 -20.027 -9.337  1.00 17.29 ?  148 ARG   B HG2  1 
ATOM   6240 H  HG3  . ARG   B 1 148 ? 28.146 -19.559 -7.992  1.00 17.29 ?  148 ARG   B HG3  1 
ATOM   6241 H  HD2  . ARG   B 1 148 ? 26.143 -18.093 -9.345  1.00 18.50 ?  148 ARG   B HD2  1 
ATOM   6242 H  HD3  . ARG   B 1 148 ? 25.930 -18.869 -7.972  1.00 18.50 ?  148 ARG   B HD3  1 
ATOM   6243 H  HE   . ARG   B 1 148 ? 27.006 -16.436 -8.218  1.00 18.16 ?  148 ARG   B HE   1 
ATOM   6244 H  HH11 . ARG   B 1 148 ? 26.927 -18.979 -6.070  1.00 17.44 ?  148 ARG   B HH11 1 
ATOM   6245 H  HH12 . ARG   B 1 148 ? 27.371 -18.184 -4.893  1.00 17.44 ?  148 ARG   B HH12 1 
ATOM   6246 H  HH21 . ARG   B 1 148 ? 27.692 -15.284 -6.426  1.00 17.21 ?  148 ARG   B HH21 1 
ATOM   6247 H  HH22 . ARG   B 1 148 ? 27.834 -15.956 -5.106  1.00 17.21 ?  148 ARG   B HH22 1 
ATOM   6248 N  N    . THR   B 1 149 ? 32.146 -18.209 -10.335 1.00 13.10 ?  149 THR   B N    1 
ATOM   6249 C  CA   . THR   B 1 149 ? 33.190 -17.649 -11.182 1.00 13.50 ?  149 THR   B CA   1 
ATOM   6250 C  C    . THR   B 1 149 ? 34.070 -18.791 -11.697 1.00 12.85 ?  149 THR   B C    1 
ATOM   6251 O  O    . THR   B 1 149 ? 33.872 -19.962 -11.362 1.00 13.37 ?  149 THR   B O    1 
ATOM   6252 C  CB   . THR   B 1 149 ? 33.962 -16.592 -10.399 1.00 13.42 ?  149 THR   B CB   1 
ATOM   6253 O  OG1  . THR   B 1 149 ? 34.421 -17.190 -9.186  1.00 13.37 ?  149 THR   B OG1  1 
ATOM   6254 C  CG2  . THR   B 1 149 ? 33.066 -15.389 -10.100 1.00 13.86 ?  149 THR   B CG2  1 
ATOM   6255 H  H    . THR   B 1 149 ? 32.306 -18.134 -9.495  1.00 15.70 ?  149 THR   B H    1 
ATOM   6256 H  HA   . THR   B 1 149 ? 32.781 -17.213 -11.945 1.00 16.18 ?  149 THR   B HA   1 
ATOM   6257 H  HB   . THR   B 1 149 ? 34.723 -16.299 -10.912 1.00 16.08 ?  149 THR   B HB   1 
ATOM   6258 H  HG1  . THR   B 1 149 ? 34.834 -16.618 -8.719  1.00 16.03 ?  149 THR   B HG1  1 
ATOM   6259 H  HG21 . THR   B 1 149 ? 33.569 -14.714 -9.614  1.00 16.61 ?  149 THR   B HG21 1 
ATOM   6260 H  HG22 . THR   B 1 149 ? 32.745 -15.002 -10.929 1.00 16.61 ?  149 THR   B HG22 1 
ATOM   6261 H  HG23 . THR   B 1 149 ? 32.305 -15.660 -9.563  1.00 16.61 ?  149 THR   B HG23 1 
ATOM   6262 N  N    . ASN   B 1 150 ? 35.038 -18.469 -12.545 1.00 13.03 ?  150 ASN   B N    1 
ATOM   6263 C  CA   . ASN   B 1 150 ? 35.801 -19.495 -13.247 1.00 13.40 ?  150 ASN   B CA   1 
ATOM   6264 C  C    . ASN   B 1 150 ? 36.968 -19.944 -12.376 1.00 12.95 ?  150 ASN   B C    1 
ATOM   6265 O  O    . ASN   B 1 150 ? 37.897 -19.171 -12.123 1.00 13.52 ?  150 ASN   B O    1 
ATOM   6266 C  CB   . ASN   B 1 150 ? 36.269 -18.967 -14.596 1.00 15.18 ?  150 ASN   B CB   1 
ATOM   6267 C  CG   . ASN   B 1 150 ? 35.126 -18.751 -15.542 1.00 17.82 ?  150 ASN   B CG   1 
ATOM   6268 O  OD1  . ASN   B 1 150 ? 34.226 -19.577 -15.618 1.00 18.85 ?  150 ASN   B OD1  1 
ATOM   6269 N  ND2  . ASN   B 1 150 ? 35.127 -17.627 -16.240 1.00 19.41 ?  150 ASN   B ND2  1 
ATOM   6270 H  H    . ASN   B 1 150 ? 35.284 -17.662 -12.723 1.00 15.62 ?  150 ASN   B H    1 
ATOM   6271 H  HA   . ASN   B 1 150 ? 35.223 -20.261 -13.406 1.00 16.06 ?  150 ASN   B HA   1 
ATOM   6272 H  HB2  . ASN   B 1 150 ? 36.716 -18.116 -14.464 1.00 18.20 ?  150 ASN   B HB2  1 
ATOM   6273 H  HB3  . ASN   B 1 150 ? 36.873 -19.607 -14.996 1.00 18.20 ?  150 ASN   B HB3  1 
ATOM   6274 H  HD21 . ASN   B 1 150 ? 34.488 -17.458 -16.792 1.00 23.28 ?  150 ASN   B HD21 1 
ATOM   6275 H  HD22 . ASN   B 1 150 ? 35.775 -17.067 -16.152 1.00 23.28 ?  150 ASN   B HD22 1 
ATOM   6276 N  N    . VAL   B 1 151 ? 36.923 -21.191 -11.917 1.00 12.74 ?  151 VAL   B N    1 
ATOM   6277 C  CA   . VAL   B 1 151 ? 37.941 -21.718 -11.022 1.00 12.89 ?  151 VAL   B CA   1 
ATOM   6278 C  C    . VAL   B 1 151 ? 38.642 -22.893 -11.690 1.00 12.59 ?  151 VAL   B C    1 
ATOM   6279 O  O    . VAL   B 1 151 ? 37.996 -23.826 -12.194 1.00 13.80 ?  151 VAL   B O    1 
ATOM   6280 C  CB   . VAL   B 1 151 ? 37.382 -22.055 -9.625  1.00 13.86 ?  151 VAL   B CB   1 
ATOM   6281 C  CG1  . VAL   B 1 151 ? 36.209 -23.040 -9.708  1.00 14.84 ?  151 VAL   B CG1  1 
ATOM   6282 C  CG2  . VAL   B 1 151 ? 38.493 -22.555 -8.710  1.00 14.86 ?  151 VAL   B CG2  1 
ATOM   6283 H  H    . VAL   B 1 151 ? 36.300 -21.757 -12.116 1.00 15.27 ?  151 VAL   B H    1 
ATOM   6284 H  HA   . VAL   B 1 151 ? 38.607 -21.024 -10.893 1.00 15.45 ?  151 VAL   B HA   1 
ATOM   6285 H  HB   . VAL   B 1 151 ? 37.038 -21.236 -9.233  1.00 16.62 ?  151 VAL   B HB   1 
ATOM   6286 H  HG11 . VAL   B 1 151 ? 35.890 -23.231 -8.810  1.00 17.79 ?  151 VAL   B HG11 1 
ATOM   6287 H  HG12 . VAL   B 1 151 ? 35.492 -22.641 -10.231 1.00 17.79 ?  151 VAL   B HG12 1 
ATOM   6288 H  HG13 . VAL   B 1 151 ? 36.508 -23.859 -10.132 1.00 17.79 ?  151 VAL   B HG13 1 
ATOM   6289 H  HG21 . VAL   B 1 151 ? 38.147 -22.622 -7.806  1.00 17.82 ?  151 VAL   B HG21 1 
ATOM   6290 H  HG22 . VAL   B 1 151 ? 38.788 -23.425 -9.016  1.00 17.82 ?  151 VAL   B HG22 1 
ATOM   6291 H  HG23 . VAL   B 1 151 ? 39.229 -21.924 -8.735  1.00 17.82 ?  151 VAL   B HG23 1 
ATOM   6292 N  N    . TYR   B 1 152 ? 39.970 -22.806 -11.713 1.00 12.18 ?  152 TYR   B N    1 
ATOM   6293 C  CA   . TYR   B 1 152 ? 40.877 -23.787 -12.289 1.00 12.37 ?  152 TYR   B CA   1 
ATOM   6294 C  C    . TYR   B 1 152 ? 41.599 -24.462 -11.127 1.00 11.74 ?  152 TYR   B C    1 
ATOM   6295 O  O    . TYR   B 1 152 ? 42.456 -23.848 -10.479 1.00 12.44 ?  152 TYR   B O    1 
ATOM   6296 C  CB   . TYR   B 1 152 ? 41.846 -23.079 -13.238 1.00 13.28 ?  152 TYR   B CB   1 
ATOM   6297 C  CG   . TYR   B 1 152 ? 41.163 -22.614 -14.504 1.00 13.89 ?  152 TYR   B CG   1 
ATOM   6298 C  CD1  . TYR   B 1 152 ? 40.500 -21.390 -14.570 1.00 14.23 ?  152 TYR   B CD1  1 
ATOM   6299 C  CD2  . TYR   B 1 152 ? 41.153 -23.422 -15.628 1.00 15.10 ?  152 TYR   B CD2  1 
ATOM   6300 C  CE1  . TYR   B 1 152 ? 39.855 -20.991 -15.727 1.00 15.64 ?  152 TYR   B CE1  1 
ATOM   6301 C  CE2  . TYR   B 1 152 ? 40.514 -23.036 -16.785 1.00 16.03 ?  152 TYR   B CE2  1 
ATOM   6302 C  CZ   . TYR   B 1 152 ? 39.871 -21.817 -16.833 1.00 16.18 ?  152 TYR   B CZ   1 
ATOM   6303 O  OH   . TYR   B 1 152 ? 39.238 -21.446 -17.993 1.00 18.94 ?  152 TYR   B OH   1 
ATOM   6304 H  H    . TYR   B 1 152 ? 40.402 -22.140 -11.367 1.00 14.60 ?  152 TYR   B H    1 
ATOM   6305 H  HA   . TYR   B 1 152 ? 40.371 -24.456 -12.785 1.00 14.83 ?  152 TYR   B HA   1 
ATOM   6306 H  HB2  . TYR   B 1 152 ? 42.213 -22.302 -12.786 1.00 15.92 ?  152 TYR   B HB2  1 
ATOM   6307 H  HB3  . TYR   B 1 152 ? 42.558 -23.690 -13.481 1.00 15.92 ?  152 TYR   B HB3  1 
ATOM   6308 H  HD1  . TYR   B 1 152 ? 40.484 -20.832 -13.824 1.00 17.06 ?  152 TYR   B HD1  1 
ATOM   6309 H  HD2  . TYR   B 1 152 ? 41.580 -24.248 -15.598 1.00 18.11 ?  152 TYR   B HD2  1 
ATOM   6310 H  HE1  . TYR   B 1 152 ? 39.419 -20.169 -15.766 1.00 18.75 ?  152 TYR   B HE1  1 
ATOM   6311 H  HE2  . TYR   B 1 152 ? 40.522 -23.591 -17.530 1.00 19.22 ?  152 TYR   B HE2  1 
ATOM   6312 H  HH   . TYR   B 1 152 ? 38.882 -20.688 -17.897 1.00 22.71 ?  152 TYR   B HH   1 
ATOM   6313 N  N    . LEU   B 1 153 ? 41.231 -25.718 -10.857 1.00 12.17 ?  153 LEU   B N    1 
ATOM   6314 C  CA   . LEU   B 1 153 ? 41.739 -26.469 -9.716  1.00 11.94 ?  153 LEU   B CA   1 
ATOM   6315 C  C    . LEU   B 1 153 ? 42.973 -27.265 -10.114 1.00 12.15 ?  153 LEU   B C    1 
ATOM   6316 O  O    . LEU   B 1 153 ? 42.957 -27.994 -11.110 1.00 13.21 ?  153 LEU   B O    1 
ATOM   6317 C  CB   . LEU   B 1 153 ? 40.664 -27.429 -9.193  1.00 12.26 ?  153 LEU   B CB   1 
ATOM   6318 C  CG   . LEU   B 1 153 ? 39.408 -26.766 -8.624  1.00 13.19 ?  153 LEU   B CG   1 
ATOM   6319 C  CD1  . LEU   B 1 153 ? 38.290 -27.794 -8.474  1.00 14.26 ?  153 LEU   B CD1  1 
ATOM   6320 C  CD2  . LEU   B 1 153 ? 39.703 -26.099 -7.289  1.00 13.44 ?  153 LEU   B CD2  1 
ATOM   6321 H  H    . LEU   B 1 153 ? 40.655 -26.166 -11.329 1.00 14.58 ?  153 LEU   B H    1 
ATOM   6322 H  HA   . LEU   B 1 153 ? 41.970 -25.853 -9.007  1.00 14.31 ?  153 LEU   B HA   1 
ATOM   6323 H  HB2  . LEU   B 1 153 ? 40.382 -28.008 -9.916  1.00 14.70 ?  153 LEU   B HB2  1 
ATOM   6324 H  HB3  . LEU   B 1 153 ? 41.052 -27.968 -8.481  1.00 14.70 ?  153 LEU   B HB3  1 
ATOM   6325 H  HG   . LEU   B 1 153 ? 39.104 -26.074 -9.235  1.00 15.81 ?  153 LEU   B HG   1 
ATOM   6326 H  HD11 . LEU   B 1 153 ? 37.483 -27.337 -8.177  1.00 17.09 ?  153 LEU   B HD11 1 
ATOM   6327 H  HD12 . LEU   B 1 153 ? 38.136 -28.209 -9.332  1.00 17.09 ?  153 LEU   B HD12 1 
ATOM   6328 H  HD13 . LEU   B 1 153 ? 38.558 -28.452 -7.820  1.00 17.09 ?  153 LEU   B HD13 1 
ATOM   6329 H  HD21 . LEU   B 1 153 ? 38.887 -25.717 -6.930  1.00 16.11 ?  153 LEU   B HD21 1 
ATOM   6330 H  HD22 . LEU   B 1 153 ? 40.054 -26.764 -6.673  1.00 16.11 ?  153 LEU   B HD22 1 
ATOM   6331 H  HD23 . LEU   B 1 153 ? 40.364 -25.397 -7.421  1.00 16.11 ?  153 LEU   B HD23 1 
ATOM   6332 N  N    . ALA   B 1 154 ? 44.027 -27.150 -9.313  1.00 12.37 ?  154 ALA   B N    1 
ATOM   6333 C  CA   . ALA   B 1 154 ? 45.252 -27.918 -9.496  1.00 13.76 ?  154 ALA   B CA   1 
ATOM   6334 C  C    . ALA   B 1 154 ? 45.314 -28.993 -8.420  1.00 14.15 ?  154 ALA   B C    1 
ATOM   6335 O  O    . ALA   B 1 154 ? 45.246 -28.686 -7.222  1.00 15.30 ?  154 ALA   B O    1 
ATOM   6336 C  CB   . ALA   B 1 154 ? 46.476 -27.007 -9.429  1.00 14.43 ?  154 ALA   B CB   1 
ATOM   6337 H  H    . ALA   B 1 154 ? 44.050 -26.617 -8.635  1.00 14.82 ?  154 ALA   B H    1 
ATOM   6338 H  HA   . ALA   B 1 154 ? 45.239 -28.347 -10.360 1.00 16.50 ?  154 ALA   B HA   1 
ATOM   6339 H  HB1  . ALA   B 1 154 ? 47.278 -27.539 -9.551  1.00 17.30 ?  154 ALA   B HB1  1 
ATOM   6340 H  HB2  . ALA   B 1 154 ? 46.416 -26.337 -10.131 1.00 17.30 ?  154 ALA   B HB2  1 
ATOM   6341 H  HB3  . ALA   B 1 154 ? 46.504 -26.566 -8.562  1.00 17.30 ?  154 ALA   B HB3  1 
ATOM   6342 N  N    . VAL   B 1 155 ? 45.435 -30.243 -8.848  1.00 13.55 ?  155 VAL   B N    1 
ATOM   6343 C  CA   . VAL   B 1 155 ? 45.544 -31.389 -7.952  1.00 13.76 ?  155 VAL   B CA   1 
ATOM   6344 C  C    . VAL   B 1 155 ? 46.882 -32.063 -8.236  1.00 13.64 ?  155 VAL   B C    1 
ATOM   6345 O  O    . VAL   B 1 155 ? 47.114 -32.553 -9.349  1.00 15.74 ?  155 VAL   B O    1 
ATOM   6346 C  CB   . VAL   B 1 155 ? 44.386 -32.383 -8.149  1.00 15.06 ?  155 VAL   B CB   1 
ATOM   6347 C  CG1  . VAL   B 1 155 ? 44.573 -33.591 -7.241  1.00 15.09 ?  155 VAL   B CG1  1 
ATOM   6348 C  CG2  . VAL   B 1 155 ? 43.051 -31.701 -7.879  1.00 15.94 ?  155 VAL   B CG2  1 
ATOM   6349 H  H    . VAL   B 1 155 ? 45.462 -30.462 -9.679  1.00 16.24 ?  155 VAL   B H    1 
ATOM   6350 H  HA   . VAL   B 1 155 ? 45.535 -31.090 -7.029  1.00 16.50 ?  155 VAL   B HA   1 
ATOM   6351 H  HB   . VAL   B 1 155 ? 44.385 -32.692 -9.069  1.00 18.06 ?  155 VAL   B HB   1 
ATOM   6352 H  HG11 . VAL   B 1 155 ? 43.746 -34.097 -7.208  1.00 18.09 ?  155 VAL   B HG11 1 
ATOM   6353 H  HG12 . VAL   B 1 155 ? 45.285 -34.153 -7.594  1.00 18.09 ?  155 VAL   B HG12 1 
ATOM   6354 H  HG13 . VAL   B 1 155 ? 44.807 -33.287 -6.349  1.00 18.09 ?  155 VAL   B HG13 1 
ATOM   6355 H  HG21 . VAL   B 1 155 ? 42.339 -32.358 -7.969  1.00 19.11 ?  155 VAL   B HG21 1 
ATOM   6356 H  HG22 . VAL   B 1 155 ? 43.056 -31.346 -6.977  1.00 19.11 ?  155 VAL   B HG22 1 
ATOM   6357 H  HG23 . VAL   B 1 155 ? 42.924 -30.986 -8.518  1.00 19.11 ?  155 VAL   B HG23 1 
ATOM   6358 N  N    . PHE   B 1 156 ? 47.749 -32.111 -7.223  1.00 14.25 ?  156 PHE   B N    1 
ATOM   6359 C  CA   . PHE   B 1 156 ? 49.127 -32.563 -7.428  1.00 15.52 ?  156 PHE   B CA   1 
ATOM   6360 C  C    . PHE   B 1 156 ? 49.221 -34.064 -7.705  1.00 16.63 ?  156 PHE   B C    1 
ATOM   6361 O  O    . PHE   B 1 156 ? 49.934 -34.493 -8.623  1.00 18.46 ?  156 PHE   B O    1 
ATOM   6362 C  CB   . PHE   B 1 156 ? 49.956 -32.189 -6.203  1.00 15.43 ?  156 PHE   B CB   1 
ATOM   6363 C  CG   . PHE   B 1 156 ? 51.383 -32.646 -6.262  1.00 16.24 ?  156 PHE   B CG   1 
ATOM   6364 C  CD1  . PHE   B 1 156 ? 52.265 -32.098 -7.175  1.00 17.56 ?  156 PHE   B CD1  1 
ATOM   6365 C  CD2  . PHE   B 1 156 ? 51.845 -33.609 -5.390  1.00 16.72 ?  156 PHE   B CD2  1 
ATOM   6366 C  CE1  . PHE   B 1 156 ? 53.586 -32.505 -7.222  1.00 18.36 ?  156 PHE   B CE1  1 
ATOM   6367 C  CE2  . PHE   B 1 156 ? 53.165 -34.019 -5.432  1.00 18.05 ?  156 PHE   B CE2  1 
ATOM   6368 C  CZ   . PHE   B 1 156 ? 54.027 -33.471 -6.354  1.00 18.45 ?  156 PHE   B CZ   1 
ATOM   6369 H  H    . PHE   B 1 156 ? 47.563 -31.896 -6.411  1.00 17.08 ?  156 PHE   B H    1 
ATOM   6370 H  HA   . PHE   B 1 156 ? 49.494 -32.096 -8.191  1.00 18.61 ?  156 PHE   B HA   1 
ATOM   6371 H  HB2  . PHE   B 1 156 ? 49.962 -31.221 -6.117  1.00 18.50 ?  156 PHE   B HB2  1 
ATOM   6372 H  HB3  . PHE   B 1 156 ? 49.554 -32.584 -5.416  1.00 18.50 ?  156 PHE   B HB3  1 
ATOM   6373 H  HD1  . PHE   B 1 156 ? 51.969 -31.440 -7.765  1.00 21.05 ?  156 PHE   B HD1  1 
ATOM   6374 H  HD2  . PHE   B 1 156 ? 51.259 -33.986 -4.771  1.00 20.05 ?  156 PHE   B HD2  1 
ATOM   6375 H  HE1  . PHE   B 1 156 ? 54.171 -32.130 -7.843  1.00 22.01 ?  156 PHE   B HE1  1 
ATOM   6376 H  HE2  . PHE   B 1 156 ? 53.462 -34.680 -4.845  1.00 21.64 ?  156 PHE   B HE2  1 
ATOM   6377 H  HZ   . PHE   B 1 156 ? 54.914 -33.751 -6.383  1.00 22.13 ?  156 PHE   B HZ   1 
ATOM   6378 N  N    . ASP   B 1 157 ? 48.558 -34.879 -6.898  1.00 16.85 ?  157 ASP   B N    1 
ATOM   6379 C  CA   . ASP   B 1 157 ? 48.700 -36.328 -6.992  1.00 18.51 ?  157 ASP   B CA   1 
ATOM   6380 C  C    . ASP   B 1 157 ? 47.784 -36.873 -8.083  1.00 18.64 ?  157 ASP   B C    1 
ATOM   6381 O  O    . ASP   B 1 157 ? 46.559 -36.763 -7.976  1.00 18.14 ?  157 ASP   B O    1 
ATOM   6382 C  CB   . ASP   B 1 157 ? 48.336 -36.942 -5.645  1.00 20.09 ?  157 ASP   B CB   1 
ATOM   6383 C  CG   . ASP   B 1 157 ? 48.483 -38.452 -5.629  1.00 22.31 ?  157 ASP   B CG   1 
ATOM   6384 O  OD1  . ASP   B 1 157 ? 48.811 -39.051 -6.680  1.00 22.60 ?  157 ASP   B OD1  1 
ATOM   6385 O  OD2  . ASP   B 1 157 ? 48.274 -39.041 -4.550  1.00 24.13 -1 157 ASP   B OD2  1 
ATOM   6386 H  H    . ASP   B 1 157 ? 48.021 -34.621 -6.282  1.00 20.21 ?  157 ASP   B H    1 
ATOM   6387 H  HA   . ASP   B 1 157 ? 49.619 -36.560 -7.206  1.00 22.19 ?  157 ASP   B HA   1 
ATOM   6388 H  HB2  . ASP   B 1 157 ? 48.906 -36.560 -4.964  1.00 24.09 ?  157 ASP   B HB2  1 
ATOM   6389 H  HB3  . ASP   B 1 157 ? 47.405 -36.731 -5.450  1.00 24.09 ?  157 ASP   B HB3  1 
ATOM   6390 N  N    . LYS   B 1 158 ? 48.377 -37.490 -9.113  1.00 19.58 ?  158 LYS   B N    1 
ATOM   6391 C  CA   . LYS   B 1 158 ? 47.601 -38.105 -10.192 1.00 20.58 ?  158 LYS   B CA   1 
ATOM   6392 C  C    . LYS   B 1 158 ? 46.542 -39.069 -9.659  1.00 20.46 ?  158 LYS   B C    1 
ATOM   6393 O  O    . LYS   B 1 158 ? 45.438 -39.159 -10.210 1.00 20.57 ?  158 LYS   B O    1 
ATOM   6394 C  CB   . LYS   B 1 158 ? 48.546 -38.827 -11.160 1.00 22.27 ?  158 LYS   B CB   1 
ATOM   6395 C  CG   . LYS   B 1 158 ? 47.864 -39.732 -12.182 1.00 24.60 ?  158 LYS   B CG   1 
ATOM   6396 C  CD   . LYS   B 1 158 ? 47.020 -38.947 -13.165 1.00 26.97 ?  158 LYS   B CD   1 
ATOM   6397 C  CE   . LYS   B 1 158 ? 46.407 -39.864 -14.212 1.00 28.63 ?  158 LYS   B CE   1 
ATOM   6398 N  NZ   . LYS   B 1 158 ? 45.332 -39.189 -14.993 1.00 29.32 ?  158 LYS   B NZ   1 
ATOM   6399 H  H    . LYS   B 1 158 ? 49.232 -37.568 -9.209  1.00 23.48 ?  158 LYS   B H    1 
ATOM   6400 H  HA   . LYS   B 1 158 ? 47.147 -37.407 -10.691 1.00 24.67 ?  158 LYS   B HA   1 
ATOM   6401 H  HB2  . LYS   B 1 158 ? 49.050 -38.160 -11.660 1.00 26.71 ?  158 LYS   B HB2  1 
ATOM   6402 H  HB3  . LYS   B 1 158 ? 49.159 -39.376 -10.648 1.00 26.71 ?  158 LYS   B HB3  1 
ATOM   6403 H  HG2  . LYS   B 1 158 ? 48.547 -40.201 -12.687 1.00 29.51 ?  158 LYS   B HG2  1 
ATOM   6404 H  HG3  . LYS   B 1 158 ? 47.295 -40.377 -11.732 1.00 29.51 ?  158 LYS   B HG3  1 
ATOM   6405 H  HD2  . LYS   B 1 158 ? 46.301 -38.501 -12.690 1.00 32.35 ?  158 LYS   B HD2  1 
ATOM   6406 H  HD3  . LYS   B 1 158 ? 47.578 -38.296 -13.620 1.00 32.35 ?  158 LYS   B HD3  1 
ATOM   6407 H  HE2  . LYS   B 1 158 ? 47.097 -40.147 -14.832 1.00 34.35 ?  158 LYS   B HE2  1 
ATOM   6408 H  HE3  . LYS   B 1 158 ? 46.019 -40.637 -13.771 1.00 34.35 ?  158 LYS   B HE3  1 
ATOM   6409 H  HZ1  . LYS   B 1 158 ? 44.994 -39.750 -15.595 1.00 35.17 ?  158 LYS   B HZ1  1 
ATOM   6410 H  HZ2  . LYS   B 1 158 ? 44.681 -38.922 -14.447 1.00 35.17 ?  158 LYS   B HZ2  1 
ATOM   6411 H  HZ3  . LYS   B 1 158 ? 45.664 -38.478 -15.415 1.00 35.17 ?  158 LYS   B HZ3  1 
ATOM   6412 N  N    . ASN   B 1 159 ? 46.864 -39.824 -8.607  1.00 20.86 ?  159 ASN   B N    1 
ATOM   6413 C  CA   . ASN   B 1 159 ? 45.910 -40.807 -8.099  1.00 21.33 ?  159 ASN   B CA   1 
ATOM   6414 C  C    . ASN   B 1 159 ? 44.712 -40.134 -7.424  1.00 20.32 ?  159 ASN   B C    1 
ATOM   6415 O  O    . ASN   B 1 159 ? 43.577 -40.618 -7.534  1.00 20.75 ?  159 ASN   B O    1 
ATOM   6416 C  CB   . ASN   B 1 159 ? 46.615 -41.788 -7.166  1.00 23.02 ?  159 ASN   B CB   1 
ATOM   6417 C  CG   . ASN   B 1 159 ? 47.638 -42.639 -7.888  1.00 24.68 ?  159 ASN   B CG   1 
ATOM   6418 O  OD1  . ASN   B 1 159 ? 47.384 -43.136 -8.994  1.00 25.38 ?  159 ASN   B OD1  1 
ATOM   6419 N  ND2  . ASN   B 1 159 ? 48.802 -42.816 -7.268  1.00 24.99 ?  159 ASN   B ND2  1 
ATOM   6420 H  H    . ASN   B 1 159 ? 47.608 -39.779 -8.183  1.00 25.02 ?  159 ASN   B H    1 
ATOM   6421 H  HA   . ASN   B 1 159 ? 45.574 -41.314 -8.855  1.00 25.58 ?  159 ASN   B HA   1 
ATOM   6422 H  HB2  . ASN   B 1 159 ? 47.070 -41.292 -6.470  1.00 27.60 ?  159 ASN   B HB2  1 
ATOM   6423 H  HB3  . ASN   B 1 159 ? 45.957 -42.383 -6.783  1.00 27.60 ?  159 ASN   B HB3  1 
ATOM   6424 H  HD21 . ASN   B 1 159 ? 49.423 -43.290 -7.637  1.00 29.98 ?  159 ASN   B HD21 1 
ATOM   6425 H  HD22 . ASN   B 1 159 ? 48.937 -42.470 -6.491  1.00 29.98 ?  159 ASN   B HD22 1 
ATOM   6426 N  N    . LEU   B 1 160 ? 44.930 -39.010 -6.734  1.00 19.39 ?  160 LEU   B N    1 
ATOM   6427 C  CA   . LEU   B 1 160 ? 43.798 -38.269 -6.190  1.00 18.46 ?  160 LEU   B CA   1 
ATOM   6428 C  C    . LEU   B 1 160 ? 43.009 -37.601 -7.305  1.00 17.51 ?  160 LEU   B C    1 
ATOM   6429 O  O    . LEU   B 1 160 ? 41.772 -37.596 -7.284  1.00 16.97 ?  160 LEU   B O    1 
ATOM   6430 C  CB   . LEU   B 1 160 ? 44.271 -37.237 -5.169  1.00 17.92 ?  160 LEU   B CB   1 
ATOM   6431 C  CG   . LEU   B 1 160 ? 43.150 -36.331 -4.645  1.00 17.96 ?  160 LEU   B CG   1 
ATOM   6432 C  CD1  . LEU   B 1 160 ? 42.032 -37.162 -4.025  1.00 18.73 ?  160 LEU   B CD1  1 
ATOM   6433 C  CD2  . LEU   B 1 160 ? 43.695 -35.323 -3.645  1.00 17.91 ?  160 LEU   B CD2  1 
ATOM   6434 H  H    . LEU   B 1 160 ? 45.705 -38.668 -6.579  1.00 23.25 ?  160 LEU   B H    1 
ATOM   6435 H  HA   . LEU   B 1 160 ? 43.210 -38.895 -5.743  1.00 22.14 ?  160 LEU   B HA   1 
ATOM   6436 H  HB2  . LEU   B 1 160 ? 44.660 -37.707 -4.412  1.00 21.49 ?  160 LEU   B HB2  1 
ATOM   6437 H  HB3  . LEU   B 1 160 ? 44.947 -36.675 -5.584  1.00 21.49 ?  160 LEU   B HB3  1 
ATOM   6438 H  HG   . LEU   B 1 160 ? 42.777 -35.837 -5.389  1.00 21.53 ?  160 LEU   B HG   1 
ATOM   6439 H  HD11 . LEU   B 1 160 ? 41.416 -36.567 -3.578  1.00 22.46 ?  160 LEU   B HD11 1 
ATOM   6440 H  HD12 . LEU   B 1 160 ? 41.572 -37.653 -4.725  1.00 22.46 ?  160 LEU   B HD12 1 
ATOM   6441 H  HD13 . LEU   B 1 160 ? 42.418 -37.784 -3.386  1.00 22.46 ?  160 LEU   B HD13 1 
ATOM   6442 H  HD21 . LEU   B 1 160 ? 42.969 -34.750 -3.359  1.00 21.47 ?  160 LEU   B HD21 1 
ATOM   6443 H  HD22 . LEU   B 1 160 ? 44.061 -35.802 -2.886  1.00 21.47 ?  160 LEU   B HD22 1 
ATOM   6444 H  HD23 . LEU   B 1 160 ? 44.387 -34.798 -4.074  1.00 21.47 ?  160 LEU   B HD23 1 
ATOM   6445 N  N    . TYR   B 1 161 ? 43.710 -37.036 -8.293  1.00 17.78 ?  161 TYR   B N    1 
ATOM   6446 C  CA   . TYR   B 1 161 ? 43.037 -36.469 -9.456  1.00 17.56 ?  161 TYR   B CA   1 
ATOM   6447 C  C    . TYR   B 1 161 ? 42.087 -37.489 -10.074 1.00 17.45 ?  161 TYR   B C    1 
ATOM   6448 O  O    . TYR   B 1 161 ? 40.911 -37.195 -10.318 1.00 17.62 ?  161 TYR   B O    1 
ATOM   6449 C  CB   . TYR   B 1 161 ? 44.077 -35.995 -10.479 1.00 18.12 ?  161 TYR   B CB   1 
ATOM   6450 C  CG   . TYR   B 1 161 ? 43.493 -35.522 -11.792 1.00 18.63 ?  161 TYR   B CG   1 
ATOM   6451 C  CD1  . TYR   B 1 161 ? 43.099 -34.199 -11.958 1.00 18.78 ?  161 TYR   B CD1  1 
ATOM   6452 C  CD2  . TYR   B 1 161 ? 43.323 -36.397 -12.862 1.00 19.24 ?  161 TYR   B CD2  1 
ATOM   6453 C  CE1  . TYR   B 1 161 ? 42.562 -33.760 -13.144 1.00 19.88 ?  161 TYR   B CE1  1 
ATOM   6454 C  CE2  . TYR   B 1 161 ? 42.779 -35.964 -14.054 1.00 20.47 ?  161 TYR   B CE2  1 
ATOM   6455 C  CZ   . TYR   B 1 161 ? 42.402 -34.644 -14.190 1.00 20.63 ?  161 TYR   B CZ   1 
ATOM   6456 O  OH   . TYR   B 1 161 ? 41.858 -34.201 -15.371 1.00 22.53 ?  161 TYR   B OH   1 
ATOM   6457 H  H    . TYR   B 1 161 ? 44.565 -36.983 -8.318  1.00 21.32 ?  161 TYR   B H    1 
ATOM   6458 H  HA   . TYR   B 1 161 ? 42.514 -35.702 -9.180  1.00 21.05 ?  161 TYR   B HA   1 
ATOM   6459 H  HB2  . TYR   B 1 161 ? 44.573 -35.251 -10.096 1.00 21.73 ?  161 TYR   B HB2  1 
ATOM   6460 H  HB3  . TYR   B 1 161 ? 44.682 -36.724 -10.675 1.00 21.73 ?  161 TYR   B HB3  1 
ATOM   6461 H  HD1  . TYR   B 1 161 ? 43.204 -33.593 -11.257 1.00 22.52 ?  161 TYR   B HD1  1 
ATOM   6462 H  HD2  . TYR   B 1 161 ? 43.573 -37.287 -12.773 1.00 23.07 ?  161 TYR   B HD2  1 
ATOM   6463 H  HE1  . TYR   B 1 161 ? 42.306 -32.866 -13.237 1.00 23.85 ?  161 TYR   B HE1  1 
ATOM   6464 H  HE2  . TYR   B 1 161 ? 42.670 -36.554 -14.763 1.00 24.55 ?  161 TYR   B HE2  1 
ATOM   6465 H  HH   . TYR   B 1 161 ? 41.819 -34.830 -15.925 1.00 27.01 ?  161 TYR   B HH   1 
ATOM   6466 N  N    . ASP   B 1 162 ? 42.579 -38.708 -10.307 1.00 17.95 ?  162 ASP   B N    1 
ATOM   6467 C  CA   . ASP   B 1 162 ? 41.748 -39.741 -10.917 1.00 18.49 ?  162 ASP   B CA   1 
ATOM   6468 C  C    . ASP   B 1 162 ? 40.544 -40.076 -10.044 1.00 18.02 ?  162 ASP   B C    1 
ATOM   6469 O  O    . ASP   B 1 162 ? 39.436 -40.290 -10.554 1.00 18.40 ?  162 ASP   B O    1 
ATOM   6470 C  CB   . ASP   B 1 162 ? 42.576 -41.005 -11.165 1.00 19.86 ?  162 ASP   B CB   1 
ATOM   6471 C  CG   . ASP   B 1 162 ? 43.584 -40.848 -12.290 1.00 21.63 ?  162 ASP   B CG   1 
ATOM   6472 O  OD1  . ASP   B 1 162 ? 43.459 -39.908 -13.098 1.00 22.02 ?  162 ASP   B OD1  1 
ATOM   6473 O  OD2  . ASP   B 1 162 ? 44.497 -41.695 -12.380 1.00 23.17 -1 162 ASP   B OD2  1 
ATOM   6474 H  H    . ASP   B 1 162 ? 43.381 -38.954 -10.126 1.00 21.52 ?  162 ASP   B H    1 
ATOM   6475 H  HA   . ASP   B 1 162 ? 41.421 -39.426 -11.772 1.00 22.17 ?  162 ASP   B HA   1 
ATOM   6476 H  HB2  . ASP   B 1 162 ? 43.074 -41.223 -10.363 1.00 23.81 ?  162 ASP   B HB2  1 
ATOM   6477 H  HB3  . ASP   B 1 162 ? 41.981 -41.734 -11.397 1.00 23.81 ?  162 ASP   B HB3  1 
ATOM   6478 N  N    . LYS   B 1 163 ? 40.741 -40.147 -8.725  1.00 17.57 ?  163 LYS   B N    1 
ATOM   6479 C  CA   . LYS   B 1 163 ? 39.619 -40.423 -7.835  1.00 18.07 ?  163 LYS   B CA   1 
ATOM   6480 C  C    . LYS   B 1 163 ? 38.576 -39.312 -7.896  1.00 16.61 ?  163 LYS   B C    1 
ATOM   6481 O  O    . LYS   B 1 163 ? 37.365 -39.581 -7.888  1.00 17.29 ?  163 LYS   B O    1 
ATOM   6482 C  CB   . LYS   B 1 163 ? 40.106 -40.602 -6.400  1.00 21.28 ?  163 LYS   B CB   1 
ATOM   6483 C  CG   . LYS   B 1 163 ? 39.021 -41.120 -5.482  1.00 26.78 ?  163 LYS   B CG   1 
ATOM   6484 C  CD   . LYS   B 1 163 ? 39.479 -41.264 -4.045  1.00 31.97 ?  163 LYS   B CD   1 
ATOM   6485 C  CE   . LYS   B 1 163 ? 38.401 -41.952 -3.217  1.00 35.67 ?  163 LYS   B CE   1 
ATOM   6486 N  NZ   . LYS   B 1 163 ? 38.485 -41.615 -1.770  1.00 38.17 ?  163 LYS   B NZ   1 
ATOM   6487 H  H    . LYS   B 1 163 ? 41.501 -40.036 -8.334  1.00 21.07 ?  163 LYS   B H    1 
ATOM   6488 H  HA   . LYS   B 1 163 ? 39.197 -41.247 -8.115  1.00 21.67 ?  163 LYS   B HA   1 
ATOM   6489 H  HB2  . LYS   B 1 163 ? 40.838 -41.240 -6.393  1.00 25.52 ?  163 LYS   B HB2  1 
ATOM   6490 H  HB3  . LYS   B 1 163 ? 40.408 -39.747 -6.058  1.00 25.52 ?  163 LYS   B HB3  1 
ATOM   6491 H  HG2  . LYS   B 1 163 ? 38.272 -40.505 -5.495  1.00 32.12 ?  163 LYS   B HG2  1 
ATOM   6492 H  HG3  . LYS   B 1 163 ? 38.736 -41.995 -5.794  1.00 32.12 ?  163 LYS   B HG3  1 
ATOM   6493 H  HD2  . LYS   B 1 163 ? 40.284 -41.806 -4.014  1.00 38.34 ?  163 LYS   B HD2  1 
ATOM   6494 H  HD3  . LYS   B 1 163 ? 39.646 -40.387 -3.669  1.00 38.34 ?  163 LYS   B HD3  1 
ATOM   6495 H  HE2  . LYS   B 1 163 ? 37.527 -41.687 -3.545  1.00 42.78 ?  163 LYS   B HE2  1 
ATOM   6496 H  HE3  . LYS   B 1 163 ? 38.504 -42.912 -3.306  1.00 42.78 ?  163 LYS   B HE3  1 
ATOM   6497 H  HZ1  . LYS   B 1 163 ? 37.839 -42.034 -1.323  1.00 45.79 ?  163 LYS   B HZ1  1 
ATOM   6498 H  HZ2  . LYS   B 1 163 ? 39.273 -41.868 -1.444  1.00 45.79 ?  163 LYS   B HZ2  1 
ATOM   6499 H  HZ3  . LYS   B 1 163 ? 38.392 -40.737 -1.656  1.00 45.79 ?  163 LYS   B HZ3  1 
ATOM   6500 N  N    . LEU   B 1 164 ? 39.032 -38.058 -7.947  1.00 15.62 ?  164 LEU   B N    1 
ATOM   6501 C  CA   . LEU   B 1 164 ? 38.122 -36.918 -8.009  1.00 15.49 ?  164 LEU   B CA   1 
ATOM   6502 C  C    . LEU   B 1 164 ? 37.341 -36.910 -9.318  1.00 15.81 ?  164 LEU   B C    1 
ATOM   6503 O  O    . LEU   B 1 164 ? 36.117 -36.720 -9.324  1.00 16.86 ?  164 LEU   B O    1 
ATOM   6504 C  CB   . LEU   B 1 164 ? 38.924 -35.628 -7.848  1.00 14.87 ?  164 LEU   B CB   1 
ATOM   6505 C  CG   . LEU   B 1 164 ? 39.455 -35.346 -6.443  1.00 15.51 ?  164 LEU   B CG   1 
ATOM   6506 C  CD1  . LEU   B 1 164 ? 40.537 -34.280 -6.496  1.00 15.04 ?  164 LEU   B CD1  1 
ATOM   6507 C  CD2  . LEU   B 1 164 ? 38.336 -34.909 -5.519  1.00 17.31 ?  164 LEU   B CD2  1 
ATOM   6508 H  H    . LEU   B 1 164 ? 39.868 -37.842 -7.945  1.00 18.72 ?  164 LEU   B H    1 
ATOM   6509 H  HA   . LEU   B 1 164 ? 37.491 -36.976 -7.284  1.00 18.57 ?  164 LEU   B HA   1 
ATOM   6510 H  HB2  . LEU   B 1 164 ? 39.693 -35.665 -8.445  1.00 17.83 ?  164 LEU   B HB2  1 
ATOM   6511 H  HB3  . LEU   B 1 164 ? 38.361 -34.883 -8.099  1.00 17.83 ?  164 LEU   B HB3  1 
ATOM   6512 H  HG   . LEU   B 1 164 ? 39.854 -36.152 -6.083  1.00 18.60 ?  164 LEU   B HG   1 
ATOM   6513 H  HD11 . LEU   B 1 164 ? 40.861 -34.105 -5.595  1.00 18.03 ?  164 LEU   B HD11 1 
ATOM   6514 H  HD12 . LEU   B 1 164 ? 41.275 -34.594 -7.049  1.00 18.03 ?  164 LEU   B HD12 1 
ATOM   6515 H  HD13 . LEU   B 1 164 ? 40.170 -33.465 -6.875  1.00 18.03 ?  164 LEU   B HD13 1 
ATOM   6516 H  HD21 . LEU   B 1 164 ? 38.708 -34.683 -4.653  1.00 20.76 ?  164 LEU   B HD21 1 
ATOM   6517 H  HD22 . LEU   B 1 164 ? 37.893 -34.135 -5.901  1.00 20.76 ?  164 LEU   B HD22 1 
ATOM   6518 H  HD23 . LEU   B 1 164 ? 37.703 -35.639 -5.427  1.00 20.76 ?  164 LEU   B HD23 1 
ATOM   6519 N  N    . VAL   B 1 165 ? 38.036 -37.086 -10.443 1.00 17.36 ?  165 VAL   B N    1 
ATOM   6520 C  CA   . VAL   B 1 165 ? 37.381 -37.030 -11.746 1.00 18.62 ?  165 VAL   B CA   1 
ATOM   6521 C  C    . VAL   B 1 165 ? 36.456 -38.226 -11.928 1.00 20.45 ?  165 VAL   B C    1 
ATOM   6522 O  O    . VAL   B 1 165 ? 35.296 -38.085 -12.334 1.00 21.84 ?  165 VAL   B O    1 
ATOM   6523 C  CB   . VAL   B 1 165 ? 38.429 -36.948 -12.872 1.00 19.62 ?  165 VAL   B CB   1 
ATOM   6524 C  CG1  . VAL   B 1 165 ? 37.767 -37.073 -14.226 1.00 20.83 ?  165 VAL   B CG1  1 
ATOM   6525 C  CG2  . VAL   B 1 165 ? 39.209 -35.649 -12.780 1.00 19.49 ?  165 VAL   B CG2  1 
ATOM   6526 H  H    . VAL   B 1 165 ? 38.888 -37.238 -10.479 1.00 20.82 ?  165 VAL   B H    1 
ATOM   6527 H  HA   . VAL   B 1 165 ? 36.843 -36.230 -11.792 1.00 22.32 ?  165 VAL   B HA   1 
ATOM   6528 H  HB   . VAL   B 1 165 ? 39.064 -37.677 -12.777 1.00 23.53 ?  165 VAL   B HB   1 
ATOM   6529 H  HG11 . VAL   B 1 165 ? 38.384 -36.773 -14.910 1.00 24.98 ?  165 VAL   B HG11 1 
ATOM   6530 H  HG12 . VAL   B 1 165 ? 37.540 -38.005 -14.378 1.00 24.98 ?  165 VAL   B HG12 1 
ATOM   6531 H  HG13 . VAL   B 1 165 ? 36.967 -36.530 -14.236 1.00 24.98 ?  165 VAL   B HG13 1 
ATOM   6532 H  HG21 . VAL   B 1 165 ? 39.841 -35.602 -13.517 1.00 23.37 ?  165 VAL   B HG21 1 
ATOM   6533 H  HG22 . VAL   B 1 165 ? 38.589 -34.903 -12.833 1.00 23.37 ?  165 VAL   B HG22 1 
ATOM   6534 H  HG23 . VAL   B 1 165 ? 39.686 -35.622 -11.936 1.00 23.37 ?  165 VAL   B HG23 1 
ATOM   6535 N  N    . SER   B 1 166 ? 36.961 -39.427 -11.626 1.00 21.13 ?  166 SER   B N    1 
ATOM   6536 C  CA   . SER   B 1 166 ? 36.205 -40.639 -11.914 1.00 22.38 ?  166 SER   B CA   1 
ATOM   6537 C  C    . SER   B 1 166 ? 34.944 -40.725 -11.070 1.00 22.54 ?  166 SER   B C    1 
ATOM   6538 O  O    . SER   B 1 166 ? 33.979 -41.363 -11.489 1.00 23.68 ?  166 SER   B O    1 
ATOM   6539 C  CB   . SER   B 1 166 ? 37.068 -41.893 -11.730 1.00 23.39 ?  166 SER   B CB   1 
ATOM   6540 O  OG   . SER   B 1 166 ? 37.425 -42.095 -10.373 1.00 23.35 ?  166 SER   B OG   1 
ATOM   6541 H  H    . SER   B 1 166 ? 37.732 -39.565 -11.262 1.00 25.34 ?  166 SER   B H    1 
ATOM   6542 H  HA   . SER   B 1 166 ? 35.932 -40.616 -12.843 1.00 26.84 ?  166 SER   B HA   1 
ATOM   6543 H  HB2  . SER   B 1 166 ? 36.568 -42.665 -12.039 1.00 28.05 ?  166 SER   B HB2  1 
ATOM   6544 H  HB3  . SER   B 1 166 ? 37.877 -41.796 -12.260 1.00 28.05 ?  166 SER   B HB3  1 
ATOM   6545 H  HG   . SER   B 1 166 ? 37.869 -41.436 -10.096 1.00 28.00 ?  166 SER   B HG   1 
ATOM   6546 N  N    . SER   B 1 167 ? 34.922 -40.102 -9.895  1.00 21.05 ?  167 SER   B N    1 
ATOM   6547 C  CA   . SER   B 1 167 ? 33.767 -40.160 -9.006  1.00 20.66 ?  167 SER   B CA   1 
ATOM   6548 C  C    . SER   B 1 167 ? 32.852 -38.941 -9.099  1.00 20.12 ?  167 SER   B C    1 
ATOM   6549 O  O    . SER   B 1 167 ? 31.775 -38.947 -8.492  1.00 20.35 ?  167 SER   B O    1 
ATOM   6550 C  CB   . SER   B 1 167 ? 34.215 -40.343 -7.550  1.00 20.58 ?  167 SER   B CB   1 
ATOM   6551 O  OG   . SER   B 1 167 ? 34.888 -39.183 -7.075  1.00 20.46 ?  167 SER   B OG   1 
ATOM   6552 H  H    . SER   B 1 167 ? 35.570 -39.640 -9.589  1.00 25.25 ?  167 SER   B H    1 
ATOM   6553 H  HA   . SER   B 1 167 ? 33.234 -40.936 -9.243  1.00 24.78 ?  167 SER   B HA   1 
ATOM   6554 H  HB2  . SER   B 1 167 ? 33.431 -40.509 -6.999  1.00 24.68 ?  167 SER   B HB2  1 
ATOM   6555 H  HB3  . SER   B 1 167 ? 34.812 -41.112 -7.502  1.00 24.68 ?  167 SER   B HB3  1 
ATOM   6556 H  HG   . SER   B 1 167 ? 35.571 -39.049 -7.540  1.00 24.54 ?  167 SER   B HG   1 
ATOM   6557 N  N    . PHE   B 1 168 ? 33.232 -37.900 -9.841  1.00 19.80 ?  168 PHE   B N    1 
ATOM   6558 C  CA   . PHE   B 1 168 ? 32.396 -36.702 -9.904  1.00 18.80 ?  168 PHE   B CA   1 
ATOM   6559 C  C    . PHE   B 1 168 ? 31.089 -36.964 -10.648 1.00 16.63 ?  168 PHE   B C    1 
ATOM   6560 O  O    . PHE   B 1 168 ? 30.042 -36.375 -10.314 1.00 17.32 ?  168 PHE   B O    1 
ATOM   6561 C  CB   . PHE   B 1 168 ? 33.163 -35.558 -10.566 1.00 19.43 ?  168 PHE   B CB   1 
ATOM   6562 C  CG   . PHE   B 1 168 ? 32.350 -34.314 -10.722 1.00 19.19 ?  168 PHE   B CG   1 
ATOM   6563 C  CD1  . PHE   B 1 168 ? 32.002 -33.562 -9.608  1.00 20.13 ?  168 PHE   B CD1  1 
ATOM   6564 C  CD2  . PHE   B 1 168 ? 31.919 -33.897 -11.967 1.00 18.74 ?  168 PHE   B CD2  1 
ATOM   6565 C  CE1  . PHE   B 1 168 ? 31.237 -32.419 -9.732  1.00 20.59 ?  168 PHE   B CE1  1 
ATOM   6566 C  CE2  . PHE   B 1 168 ? 31.166 -32.738 -12.104 1.00 19.64 ?  168 PHE   B CE2  1 
ATOM   6567 C  CZ   . PHE   B 1 168 ? 30.819 -31.998 -10.982 1.00 19.89 ?  168 PHE   B CZ   1 
ATOM   6568 H  H    . PHE   B 1 168 ? 33.954 -37.860 -10.303 1.00 23.74 ?  168 PHE   B H    1 
ATOM   6569 H  HA   . PHE   B 1 168 ? 32.167 -36.426 -9.005  1.00 22.54 ?  168 PHE   B HA   1 
ATOM   6570 H  HB2  . PHE   B 1 168 ? 33.934 -35.339 -10.022 1.00 23.29 ?  168 PHE   B HB2  1 
ATOM   6571 H  HB3  . PHE   B 1 168 ? 33.448 -35.834 -11.450 1.00 23.29 ?  168 PHE   B HB3  1 
ATOM   6572 H  HD1  . PHE   B 1 168 ? 32.277 -33.843 -8.766  1.00 24.14 ?  168 PHE   B HD1  1 
ATOM   6573 H  HD2  . PHE   B 1 168 ? 32.150 -34.382 -12.722 1.00 22.47 ?  168 PHE   B HD2  1 
ATOM   6574 H  HE1  . PHE   B 1 168 ? 31.010 -31.927 -8.977  1.00 24.69 ?  168 PHE   B HE1  1 
ATOM   6575 H  HE2  . PHE   B 1 168 ? 30.881 -32.463 -12.948 1.00 23.55 ?  168 PHE   B HE2  1 
ATOM   6576 H  HZ   . PHE   B 1 168 ? 30.306 -31.227 -11.072 1.00 23.86 ?  168 PHE   B HZ   1 
ATOM   6577 N  N    . LEU   B 1 169 ? 31.135 -37.841 -11.649 1.00 16.74 ?  169 LEU   B N    1 
ATOM   6578 C  CA   . LEU   B 1 169 ? 29.966 -38.162 -12.457 1.00 18.92 ?  169 LEU   B CA   1 
ATOM   6579 C  C    . LEU   B 1 169 ? 29.959 -39.606 -12.940 1.00 21.83 ?  169 LEU   B C    1 
ATOM   6580 O  O    . LEU   B 1 169 ? 29.056 -40.021 -13.665 1.00 24.27 ?  169 LEU   B O    1 
ATOM   6581 C  CB   . LEU   B 1 169 ? 29.889 -37.231 -13.667 1.00 20.74 ?  169 LEU   B CB   1 
ATOM   6582 C  CG   . LEU   B 1 169 ? 28.625 -36.379 -13.776 1.00 23.47 ?  169 LEU   B CG   1 
ATOM   6583 C  CD1  . LEU   B 1 169 ? 28.553 -35.764 -15.155 1.00 24.41 ?  169 LEU   B CD1  1 
ATOM   6584 C  CD2  . LEU   B 1 169 ? 27.370 -37.184 -13.479 1.00 23.27 ?  169 LEU   B CD2  1 
ATOM   6585 O  OXT  . LEU   B 1 169 ? 30.858 -40.376 -12.620 1.00 22.96 -1 169 LEU   B OXT  1 
ATOM   6586 H  H    . LEU   B 1 169 ? 31.846 -38.260 -11.892 1.00 20.07 ?  169 LEU   B H    1 
ATOM   6587 H  HA   . LEU   B 1 169 ? 29.180 -38.025 -11.915 1.00 22.69 ?  169 LEU   B HA   1 
ATOM   6588 H  HB2  . LEU   B 1 169 ? 30.642 -36.621 -13.639 1.00 24.87 ?  169 LEU   B HB2  1 
ATOM   6589 H  HB3  . LEU   B 1 169 ? 29.938 -37.766 -14.475 1.00 24.87 ?  169 LEU   B HB3  1 
ATOM   6590 H  HG   . LEU   B 1 169 ? 28.675 -35.654 -13.131 1.00 28.15 ?  169 LEU   B HG   1 
ATOM   6591 H  HD11 . LEU   B 1 169 ? 27.767 -35.198 -15.206 1.00 29.27 ?  169 LEU   B HD11 1 
ATOM   6592 H  HD12 . LEU   B 1 169 ? 29.352 -35.238 -15.306 1.00 29.27 ?  169 LEU   B HD12 1 
ATOM   6593 H  HD13 . LEU   B 1 169 ? 28.493 -36.475 -15.811 1.00 29.27 ?  169 LEU   B HD13 1 
ATOM   6594 H  HD21 . LEU   B 1 169 ? 26.615 -36.773 -13.921 1.00 27.90 ?  169 LEU   B HD21 1 
ATOM   6595 H  HD22 . LEU   B 1 169 ? 27.494 -38.091 -13.808 1.00 27.90 ?  169 LEU   B HD22 1 
ATOM   6596 H  HD23 . LEU   B 1 169 ? 27.228 -37.200 -12.520 1.00 27.90 ?  169 LEU   B HD23 1 
HETATM 6597 C  C1   T TFA   C 2 .   ? 12.135 -1.323  1.464   0.30 10.92 ?  201 TFA   A C1   1 
HETATM 6598 C  C2   T TFA   C 2 .   ? 12.766 -1.737  0.110   0.30 13.23 ?  201 TFA   A C2   1 
HETATM 6599 O  O    T TFA   C 2 .   ? 12.860 -1.566  2.435   0.30 9.51  ?  201 TFA   A O    1 
HETATM 6600 F  F1   T TFA   C 2 .   ? 12.855 -3.078  0.053   0.30 14.41 ?  201 TFA   A F1   1 
HETATM 6601 F  F2   T TFA   C 2 .   ? 12.046 -1.372  -0.962  0.30 13.93 ?  201 TFA   A F2   1 
HETATM 6602 F  F3   T TFA   C 2 .   ? 13.989 -1.227  -0.073  0.30 14.28 ?  201 TFA   A F3   1 
HETATM 6603 O  OXT  T TFA   C 2 .   ? 11.016 -0.816  1.397   0.30 11.17 ?  201 TFA   A OXT  1 
HETATM 6604 N  N2   B A1A6Y D 3 .   ? 15.076 0.835   1.658   0.30 12.99 ?  202 A1A6Y A N2   1 
HETATM 6605 C  C3   B A1A6Y D 3 .   ? 14.021 -0.042  -0.452  0.30 15.40 ?  202 A1A6Y A C3   1 
HETATM 6606 C  C6   B A1A6Y D 3 .   ? 10.774 2.294   -0.049  0.30 16.75 ?  202 A1A6Y A C6   1 
HETATM 6607 C  C9   B A1A6Y D 3 .   ? 15.386 2.085   5.159   0.30 12.01 ?  202 A1A6Y A C9   1 
HETATM 6608 C  C12  B A1A6Y D 3 .   ? 15.839 4.220   4.651   0.30 11.25 ?  202 A1A6Y A C12  1 
HETATM 6609 C  C1   B A1A6Y D 3 .   ? 15.987 -1.257  0.612   0.30 14.92 ?  202 A1A6Y A C1   1 
HETATM 6610 C  C10  B A1A6Y D 3 .   ? 15.387 2.169   3.728   0.30 12.29 ?  202 A1A6Y A C10  1 
HETATM 6611 C  C11  B A1A6Y D 3 .   ? 15.692 3.558   3.443   0.30 11.81 ?  202 A1A6Y A C11  1 
HETATM 6612 C  C2   B A1A6Y D 3 .   ? 14.724 -0.387  0.928   0.30 14.38 ?  202 A1A6Y A C2   1 
HETATM 6613 C  C4   B A1A6Y D 3 .   ? 12.713 0.715   -0.402  0.30 16.24 ?  202 A1A6Y A C4   1 
HETATM 6614 C  C5   B A1A6Y D 3 .   ? 11.522 0.406   -1.027  0.30 16.50 ?  202 A1A6Y A C5   1 
HETATM 6615 C  C7   B A1A6Y D 3 .   ? 15.117 0.947   3.045   0.30 12.95 ?  202 A1A6Y A C7   1 
HETATM 6616 C  C8   B A1A6Y D 3 .   ? 14.912 -0.115  5.148   0.30 13.21 ?  202 A1A6Y A C8   1 
HETATM 6617 N  N1   B A1A6Y D 3 .   ? 10.432 1.290   -0.832  0.30 16.77 ?  202 A1A6Y A N1   1 
HETATM 6618 N  N3   B A1A6Y D 3 .   ? 14.883 -0.184  3.776   0.30 13.45 ?  202 A1A6Y A N3   1 
HETATM 6619 N  N4   B A1A6Y D 3 .   ? 15.151 0.960   5.897   0.30 12.83 ?  202 A1A6Y A N4   1 
HETATM 6620 N  N5   B A1A6Y D 3 .   ? 15.662 3.314   5.665   0.30 11.01 ?  202 A1A6Y A N5   1 
HETATM 6621 O  O1   B A1A6Y D 3 .   ? 15.549 -2.408  -0.045  0.30 15.23 ?  202 A1A6Y A O1   1 
HETATM 6622 S  S1   B A1A6Y D 3 .   ? 12.443 2.213   0.481   0.30 16.77 ?  202 A1A6Y A S1   1 
HETATM 6623 H  H9   B A1A6Y D 3 .   ? 15.303 1.656   1.111   0.30 15.57 ?  202 A1A6Y A H9   1 
HETATM 6624 H  H6   B A1A6Y D 3 .   ? 14.740 0.497   -1.044  0.30 18.46 ?  202 A1A6Y A H6   1 
HETATM 6625 H  H5   B A1A6Y D 3 .   ? 13.864 -0.977  -1.053  0.30 18.46 ?  202 A1A6Y A H5   1 
HETATM 6626 H  H8   B A1A6Y D 3 .   ? 10.080 3.075   0.220   0.30 20.08 ?  202 A1A6Y A H8   1 
HETATM 6627 H  H12  B A1A6Y D 3 .   ? 16.069 5.246   4.911   0.30 13.48 ?  202 A1A6Y A H12  1 
HETATM 6628 H  H3   B A1A6Y D 3 .   ? 16.759 -0.725  0.012   0.30 17.89 ?  202 A1A6Y A H3   1 
HETATM 6629 H  H4   B A1A6Y D 3 .   ? 16.500 -1.535  1.559   0.30 17.89 ?  202 A1A6Y A H4   1 
HETATM 6630 H  H11  B A1A6Y D 3 .   ? 15.780 4.037   2.492   0.30 14.15 ?  202 A1A6Y A H11  1 
HETATM 6631 H  H1   B A1A6Y D 3 .   ? 13.994 -0.969  1.533   0.30 17.24 ?  202 A1A6Y A H1   1 
HETATM 6632 H  H7   B A1A6Y D 3 .   ? 11.250 -0.432  -1.675  0.30 19.79 ?  202 A1A6Y A H7   1 
HETATM 6633 H  H10  B A1A6Y D 3 .   ? 14.719 -1.023  5.741   0.30 15.83 ?  202 A1A6Y A H10  1 
HETATM 6634 H  H13  B A1A6Y D 3 .   ? 15.717 3.523   6.698   0.30 13.19 ?  202 A1A6Y A H13  1 
HETATM 6635 H  H2   B A1A6Y D 3 .   ? 16.325 -2.875  -0.384  0.30 18.26 ?  202 A1A6Y A H2   1 
HETATM 6636 CL CL   B CL    E 4 .   ? 16.107 2.714   -1.153  0.30 16.20 ?  203 CL    A CL   1 
HETATM 6637 O  O    . HOH   F 5 .   ? 7.927  -12.534 -0.879  1.00 22.53 ?  301 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 5 .   ? 14.720 -4.628  20.498  1.00 44.84 ?  302 HOH   A O    1 
HETATM 6639 O  O    . HOH   F 5 .   ? 18.626 -2.368  -16.439 1.00 45.49 ?  303 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 5 .   ? 17.105 -18.007 15.003  1.00 26.34 ?  304 HOH   A O    1 
HETATM 6641 O  O    . HOH   F 5 .   ? 7.661  -6.316  -6.649  1.00 38.94 ?  305 HOH   A O    1 
HETATM 6642 O  O    . HOH   F 5 .   ? 34.291 -1.854  12.529  1.00 37.12 ?  306 HOH   A O    1 
HETATM 6643 O  O    B HOH   F 5 .   ? 4.638  4.245   0.880   0.30 36.59 ?  307 HOH   A O    1 
HETATM 6644 O  O    A HOH   F 5 .   ? 4.697  3.934   0.578   0.70 21.49 ?  308 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 5 .   ? 11.994 0.349   14.741  1.00 32.42 ?  309 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 5 .   ? 9.287  -10.127 19.428  1.00 39.39 ?  310 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 5 .   ? 15.081 -12.235 18.617  1.00 38.97 ?  311 HOH   A O    1 
HETATM 6648 O  O    B HOH   F 5 .   ? 15.330 6.855   6.945   0.30 19.03 ?  312 HOH   A O    1 
HETATM 6649 O  O    . HOH   F 5 .   ? 28.941 0.462   -9.717  1.00 22.24 ?  313 HOH   A O    1 
HETATM 6650 O  O    . HOH   F 5 .   ? 11.702 -10.873 -10.115 1.00 44.82 ?  314 HOH   A O    1 
HETATM 6651 O  O    . HOH   F 5 .   ? 14.673 -13.927 16.653  1.00 26.79 ?  315 HOH   A O    1 
HETATM 6652 O  O    . HOH   F 5 .   ? 30.966 6.221   -12.267 1.00 28.79 ?  316 HOH   A O    1 
HETATM 6653 O  O    . HOH   F 5 .   ? 14.148 -4.492  -11.923 1.00 34.05 ?  317 HOH   A O    1 
HETATM 6654 O  O    . HOH   F 5 .   ? 42.428 10.558  5.114   1.00 20.61 ?  318 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 30.237 -13.310 -8.523  1.00 24.96 ?  319 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 16.172 16.630  8.605   1.00 33.78 ?  320 HOH   A O    1 
HETATM 6657 O  O    . HOH   F 5 .   ? 13.261 -1.453  -6.690  1.00 17.70 ?  321 HOH   A O    1 
HETATM 6658 O  O    B HOH   F 5 .   ? 22.684 5.729   -1.679  0.30 20.13 ?  322 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 5 .   ? -0.665 -8.546  2.146   1.00 43.44 ?  323 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 21.300 -2.290  -2.375  1.00 16.53 ?  324 HOH   A O    1 
HETATM 6661 O  O    A HOH   F 5 .   ? 3.593  -9.438  9.704   0.70 24.48 ?  325 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 5 .   ? 19.916 -12.535 -8.893  1.00 25.42 ?  326 HOH   A O    1 
HETATM 6663 O  O    A HOH   F 5 .   ? 6.941  -8.135  11.823  0.70 17.04 ?  327 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 26.486 -19.322 -1.773  1.00 14.55 ?  328 HOH   A O    1 
HETATM 6665 O  O    . HOH   F 5 .   ? 15.113 4.081   17.644  1.00 42.05 ?  329 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 5 .   ? 28.157 -6.261  19.634  1.00 42.27 ?  330 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 5 .   ? 34.031 -1.039  -8.898  1.00 27.38 ?  331 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 22.728 12.520  1.602   1.00 14.94 ?  332 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 36.188 -5.078  -0.528  1.00 31.86 ?  333 HOH   A O    1 
HETATM 6670 O  O    . HOH   F 5 .   ? 38.274 10.169  7.134   1.00 46.51 ?  334 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 28.402 -0.156  -13.411 1.00 35.73 ?  335 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 5 .   ? -0.416 -2.902  3.041   1.00 40.16 ?  336 HOH   A O    1 
HETATM 6673 O  O    B HOH   F 5 .   ? 11.048 -1.028  2.309   0.30 25.51 ?  337 HOH   A O    1 
HETATM 6674 O  O    . HOH   F 5 .   ? 37.523 2.818   10.221  1.00 28.59 ?  338 HOH   A O    1 
HETATM 6675 O  O    A HOH   F 5 .   ? 14.635 -3.639  3.073   0.70 15.02 ?  339 HOH   A O    1 
HETATM 6676 O  O    . HOH   F 5 .   ? 0.630  -4.446  0.102   1.00 32.01 ?  340 HOH   A O    1 
HETATM 6677 O  O    . HOH   F 5 .   ? 13.534 -15.215 -7.498  1.00 24.90 ?  341 HOH   A O    1 
HETATM 6678 O  O    B HOH   F 5 .   ? 11.044 2.072   11.908  0.30 20.74 ?  342 HOH   A O    1 
HETATM 6679 O  O    . HOH   F 5 .   ? 31.020 -18.119 7.827   1.00 20.38 ?  343 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 5 .   ? 44.330 7.152   6.410   1.00 26.24 ?  344 HOH   A O    1 
HETATM 6681 O  O    . HOH   F 5 .   ? 27.324 13.803  2.842   1.00 30.73 ?  345 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 5 .   ? 27.940 0.820   -7.141  1.00 14.29 ?  346 HOH   A O    1 
HETATM 6683 O  O    . HOH   F 5 .   ? 22.293 5.394   18.993  1.00 44.45 ?  347 HOH   A O    1 
HETATM 6684 O  O    . HOH   F 5 .   ? 18.650 -19.369 13.551  1.00 37.17 ?  348 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 5 .   ? 20.662 -19.754 -5.066  1.00 26.46 ?  349 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 5 .   ? 9.874  -21.397 5.668   1.00 19.01 ?  350 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 5 .   ? 18.876 -21.975 6.938   1.00 31.78 ?  351 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 5 .   ? 39.771 -1.045  -5.166  1.00 22.45 ?  352 HOH   A O    1 
HETATM 6689 O  O    . HOH   F 5 .   ? 26.864 11.432  1.634   1.00 16.68 ?  353 HOH   A O    1 
HETATM 6690 O  O    . HOH   F 5 .   ? 38.573 4.988   6.994   1.00 15.25 ?  354 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 5 .   ? 42.581 4.295   5.443   1.00 32.75 ?  355 HOH   A O    1 
HETATM 6692 O  O    B HOH   F 5 .   ? 7.987  3.918   1.350   0.30 19.47 ?  356 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 5 .   ? 15.498 11.861  7.878   1.00 39.82 ?  357 HOH   A O    1 
HETATM 6694 O  O    A HOH   F 5 .   ? 14.274 0.592   6.771   0.70 18.13 ?  358 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 5 .   ? 11.680 -10.721 16.958  1.00 25.02 ?  359 HOH   A O    1 
HETATM 6696 O  O    . HOH   F 5 .   ? 24.047 -2.100  -2.094  1.00 11.05 ?  360 HOH   A O    1 
HETATM 6697 O  O    . HOH   F 5 .   ? 14.362 -21.214 -4.251  1.00 29.94 ?  361 HOH   A O    1 
HETATM 6698 O  O    A HOH   F 5 .   ? 8.182  -21.379 3.978   0.70 36.54 ?  362 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 5 .   ? 35.774 -12.642 6.840   1.00 16.20 ?  363 HOH   A O    1 
HETATM 6700 O  O    . HOH   F 5 .   ? 17.157 -17.753 -5.013  1.00 26.67 ?  364 HOH   A O    1 
HETATM 6701 O  O    B HOH   F 5 .   ? 14.842 -2.934  3.350   0.30 16.96 ?  365 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 5 .   ? 14.484 -24.681 11.603  1.00 41.95 ?  366 HOH   A O    1 
HETATM 6703 O  O    . HOH   F 5 .   ? 31.694 8.219   14.873  1.00 24.63 ?  367 HOH   A O    1 
HETATM 6704 O  O    . HOH   F 5 .   ? 31.092 -13.943 -2.477  1.00 14.58 ?  368 HOH   A O    1 
HETATM 6705 O  O    . HOH   F 5 .   ? 22.137 -19.231 11.408  1.00 36.83 ?  369 HOH   A O    1 
HETATM 6706 O  O    . HOH   F 5 .   ? 43.971 8.425   -3.059  1.00 27.89 ?  370 HOH   A O    1 
HETATM 6707 O  O    A HOH   F 5 .   ? 17.498 -1.702  0.418   0.70 18.27 ?  371 HOH   A O    1 
HETATM 6708 O  O    . HOH   F 5 .   ? 30.801 3.103   8.274   1.00 12.35 ?  372 HOH   A O    1 
HETATM 6709 O  O    A HOH   F 5 .   ? 11.069 -0.364  1.904   0.40 19.47 ?  373 HOH   A O    1 
HETATM 6710 O  O    B HOH   F 5 .   ? 18.812 -1.015  -1.585  0.30 11.99 ?  374 HOH   A O    1 
HETATM 6711 O  O    . HOH   F 5 .   ? 21.888 -21.907 8.480   1.00 28.73 ?  375 HOH   A O    1 
HETATM 6712 O  O    . HOH   F 5 .   ? 31.893 -9.345  -6.651  1.00 22.45 ?  376 HOH   A O    1 
HETATM 6713 O  O    . HOH   F 5 .   ? 43.388 7.809   2.716   1.00 29.43 ?  377 HOH   A O    1 
HETATM 6714 O  O    . HOH   F 5 .   ? 37.355 11.993  4.945   1.00 28.91 ?  378 HOH   A O    1 
HETATM 6715 O  O    . HOH   F 5 .   ? 33.637 -7.139  4.330   1.00 16.87 ?  379 HOH   A O    1 
HETATM 6716 O  O    . HOH   F 5 .   ? 37.247 -2.815  9.728   1.00 42.15 ?  380 HOH   A O    1 
HETATM 6717 O  O    . HOH   F 5 .   ? 25.709 -0.791  -7.354  1.00 15.94 ?  381 HOH   A O    1 
HETATM 6718 O  O    . HOH   F 5 .   ? 27.436 -10.596 14.062  1.00 18.07 ?  382 HOH   A O    1 
HETATM 6719 O  O    . HOH   F 5 .   ? 18.580 9.503   8.981   1.00 21.16 ?  383 HOH   A O    1 
HETATM 6720 O  O    . HOH   F 5 .   ? 21.191 10.245  14.987  1.00 34.68 ?  384 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 16.531 -22.055 0.966   1.00 28.24 ?  385 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 5 .   ? 31.821 -7.299  -9.828  1.00 21.83 ?  386 HOH   A O    1 
HETATM 6723 O  O    T HOH   F 5 .   ? 15.408 -0.407  2.359   0.30 11.84 ?  387 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 5 .   ? 33.530 -16.951 8.110   1.00 19.72 ?  388 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 5 .   ? 24.684 -17.495 12.710  1.00 24.20 ?  389 HOH   A O    1 
HETATM 6726 O  O    B HOH   F 5 .   ? 11.893 -1.470  -3.627  0.30 18.33 ?  390 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 5 .   ? 24.574 1.999   -7.036  1.00 21.21 ?  391 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 24.427 3.589   -1.825  1.00 15.17 ?  392 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 16.987 -19.255 4.869   1.00 15.46 ?  393 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 6.698  -3.253  12.834  1.00 30.54 ?  394 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 15.181 -21.544 14.227  1.00 18.77 ?  395 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 24.151 -7.726  14.418  1.00 16.88 ?  396 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 32.761 -9.232  5.987   1.00 20.50 ?  397 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 13.905 -4.912  17.393  1.00 26.68 ?  398 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 23.929 -15.690 -9.204  1.00 37.59 ?  399 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 21.353 3.074   -0.296  1.00 13.29 ?  400 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 37.572 -2.027  5.866   1.00 27.46 ?  401 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 14.559 -0.510  -12.167 1.00 25.00 ?  402 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 22.657 -11.890 21.805  1.00 48.17 ?  403 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? -1.366 -4.948  7.599   1.00 40.44 ?  404 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 30.649 1.925   16.704  1.00 22.09 ?  405 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 14.059 -23.048 7.420   1.00 18.46 ?  406 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 15.169 -8.087  -9.764  1.00 23.50 ?  407 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 27.483 -6.079  -13.983 1.00 37.36 ?  408 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 23.486 11.395  4.058   1.00 12.64 ?  409 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 28.602 -10.628 -14.016 1.00 43.33 ?  410 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 20.542 -20.028 2.782   1.00 18.51 ?  411 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 27.262 2.352   18.705  1.00 31.83 ?  412 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 23.938 -20.271 -1.349  1.00 16.78 ?  413 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 21.769 -13.786 -8.187  1.00 43.58 ?  414 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 30.024 -10.060 13.028  1.00 22.08 ?  415 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 26.942 4.167   -0.661  1.00 12.81 ?  416 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 40.900 -8.265  -6.793  1.00 36.91 ?  417 HOH   A O    1 
HETATM 6754 O  O    A HOH   F 5 .   ? 15.799 -0.928  5.244   0.70 18.30 ?  418 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 38.133 -1.346  -1.934  1.00 19.12 ?  419 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 30.298 -12.871 13.520  1.00 20.46 ?  420 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 32.696 -4.296  -9.870  1.00 29.74 ?  421 HOH   A O    1 
HETATM 6758 O  O    A HOH   F 5 .   ? 20.108 4.547   -7.574  0.70 17.82 ?  422 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 35.113 -5.230  -3.099  1.00 18.12 ?  423 HOH   A O    1 
HETATM 6760 O  O    A HOH   F 5 .   ? 24.099 3.964   -4.941  0.70 19.45 ?  424 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 36.711 -4.970  5.399   1.00 25.41 ?  425 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 32.520 -10.641 3.223   1.00 32.16 ?  426 HOH   A O    1 
HETATM 6763 O  O    A HOH   F 5 .   ? 11.030 1.577   12.720  0.70 20.22 ?  427 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 41.625 1.511   5.046   1.00 37.22 ?  428 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 10.370 -13.715 -1.691  1.00 17.13 ?  429 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 44.962 -0.630  3.059   1.00 41.16 ?  430 HOH   A O    1 
HETATM 6767 O  O    A HOH   F 5 .   ? 6.460  -5.579  11.150  0.70 17.45 ?  431 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 15.972 6.838   2.957   1.00 18.96 ?  432 HOH   A O    1 
HETATM 6769 O  O    A HOH   F 5 .   ? 8.995  -12.092 17.168  0.70 42.73 ?  433 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 5.368  2.804   4.999   1.00 35.07 ?  434 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 16.194 -14.160 20.134  1.00 50.30 ?  435 HOH   A O    1 
HETATM 6772 O  O    A HOH   F 5 .   ? 18.963 -0.659  -1.650  0.70 13.94 ?  436 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 10.357 -22.152 -1.255  1.00 50.64 ?  437 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 22.596 8.218   18.360  1.00 48.24 ?  438 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 19.473 -11.001 24.008  1.00 69.32 ?  439 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 23.480 -7.985  17.105  1.00 21.83 ?  440 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 27.076 -3.142  19.381  1.00 37.45 ?  441 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 23.357 -20.919 1.351   1.00 18.92 ?  442 HOH   A O    1 
HETATM 6779 O  O    A HOH   F 5 .   ? 16.263 2.958   -1.470  0.70 16.25 ?  443 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 37.749 -8.846  -3.454  1.00 23.80 ?  444 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 21.264 -9.194  21.328  1.00 49.28 ?  445 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 18.383 -15.959 16.275  1.00 37.06 ?  446 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 18.879 1.948   -0.684  1.00 13.55 ?  447 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 34.409 -8.087  -0.550  1.00 27.37 ?  448 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 18.486 4.902   -15.141 1.00 48.00 ?  449 HOH   A O    1 
HETATM 6786 O  O    A HOH   F 5 .   ? 9.386  -16.313 -2.000  0.70 37.34 ?  450 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 23.204 7.597   -3.269  1.00 31.16 ?  451 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 31.328 -12.758 0.016   1.00 20.01 ?  452 HOH   A O    1 
HETATM 6789 O  O    A HOH   F 5 .   ? 14.028 -0.323  3.434   0.40 33.23 ?  453 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 21.471 -14.646 17.917  1.00 53.08 ?  454 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 20.576 -17.724 24.810  1.00 53.08 ?  455 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 30.607 14.786  2.745   1.00 18.87 ?  456 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 27.745 6.998   -6.510  1.00 38.29 ?  457 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 29.785 -1.958  -12.753 1.00 45.65 ?  458 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 29.840 -16.037 10.755  1.00 34.74 ?  459 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 16.050 2.352   24.983  1.00 47.98 ?  460 HOH   A O    1 
HETATM 6797 O  O    B HOH   F 5 .   ? 12.713 -3.289  1.524   0.30 20.94 ?  461 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 25.424 8.247   -4.846  1.00 31.40 ?  462 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 32.434 -15.931 10.867  1.00 31.01 ?  463 HOH   A O    1 
HETATM 6800 O  O    B HOH   F 5 .   ? 7.407  3.878   4.036   0.30 21.96 ?  464 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 24.816 5.640   20.725  1.00 50.90 ?  465 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 23.158 -22.264 -3.343  1.00 36.91 ?  466 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 19.883 -17.345 -5.051  1.00 23.95 ?  467 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 18.767 10.920  11.262  1.00 33.72 ?  468 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 24.646 14.615  7.768   1.00 36.34 ?  469 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 23.504 13.734  5.501   1.00 18.64 ?  470 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 39.630 -7.042  -3.540  1.00 45.65 ?  471 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 15.715 -21.500 3.686   1.00 23.34 ?  472 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 26.917 11.674  -1.359  1.00 32.94 ?  473 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 12.013 -13.400 16.382  1.00 55.46 ?  474 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 27.426 -11.365 16.579  1.00 38.03 ?  475 HOH   A O    1 
HETATM 6812 O  O    A HOH   F 5 .   ? 21.974 5.272   -5.863  0.70 28.41 ?  476 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 12.327 1.596   17.282  1.00 40.42 ?  477 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 18.093 -16.191 -8.861  1.00 42.06 ?  478 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 11.006 -15.059 -6.107  1.00 34.42 ?  479 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 25.835 10.791  -3.791  1.00 25.87 ?  480 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 15.697 -17.102 -6.998  1.00 29.61 ?  481 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 13.963 -10.372 -10.915 1.00 32.33 ?  482 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 16.810 -20.509 16.131  1.00 29.31 ?  483 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 35.181 7.509   12.227  1.00 47.67 ?  484 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 28.867 9.058   17.530  1.00 38.12 ?  485 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 23.130 11.840  -4.078  1.00 19.38 ?  486 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 17.371 -18.742 19.822  1.00 51.58 ?  487 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 28.567 -4.665  -12.302 1.00 38.04 ?  488 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 41.002 -3.983  -0.348  1.00 37.37 ?  489 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 30.850 0.742   19.105  1.00 39.35 ?  490 HOH   A O    1 
HETATM 6827 O  O    B HOH   F 5 .   ? 11.657 8.914   7.564   0.30 37.07 ?  491 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 23.212 -12.852 19.311  1.00 43.66 ?  492 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 20.504 -16.024 -7.389  1.00 28.77 ?  493 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 44.551 10.444  -1.588  1.00 30.70 ?  494 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 41.762 9.382   -3.954  1.00 31.29 ?  495 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 28.696 -7.964  -15.283 1.00 47.66 ?  496 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 39.190 2.426   7.430   1.00 32.27 ?  497 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 16.020 -6.814  -11.888 1.00 42.94 ?  498 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 18.412 -23.196 1.916   1.00 42.98 ?  499 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 13.877 -25.213 8.899   1.00 32.81 ?  500 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 31.479 -0.550  -10.573 1.00 30.81 ?  501 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 40.593 -0.261  -7.798  1.00 34.82 ?  502 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 16.182 -23.345 5.746   1.00 28.94 ?  503 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 20.031 -22.350 4.196   1.00 29.52 ?  504 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 30.716 5.817   -14.767 1.00 34.79 ?  505 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 30.774 -5.820  -11.844 1.00 44.50 ?  506 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 8.053  -3.182  -5.800  1.00 47.02 ?  507 HOH   A O    1 
HETATM 6844 O  O    B HOH   F 5 .   ? 14.775 8.106   4.846   0.30 20.25 ?  508 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 37.377 -6.633  7.630   1.00 27.73 ?  509 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 39.516 -0.020  6.614   1.00 32.14 ?  510 HOH   A O    1 
HETATM 6847 O  O    B HOH   F 5 .   ? 5.653  6.825   1.488   0.30 29.56 ?  511 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 38.017 13.966  6.699   1.00 44.59 ?  512 HOH   A O    1 
HETATM 6849 O  O    B HOH   F 5 .   ? 7.344  5.859   5.871   0.30 26.65 ?  513 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 29.010 14.454  0.820   1.00 48.65 ?  514 HOH   A O    1 
HETATM 6851 O  O    B HOH   F 5 .   ? 1.820  4.568   1.452   0.30 24.55 ?  515 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 22.015 -24.004 4.468   1.00 26.61 ?  516 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 36.491 -6.475  10.206  1.00 44.89 ?  517 HOH   A O    1 
HETATM 6854 O  O    T HOH   F 5 .   ? 11.927 -2.138  -3.682  0.30 12.16 ?  518 HOH   A O    1 
HETATM 6855 O  O    A HOH   F 5 .   ? 14.853 8.668   4.854   0.70 46.42 ?  519 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 17.154 -6.979  -14.305 1.00 44.57 ?  520 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 24.094 9.050   -7.236  1.00 37.96 ?  521 HOH   A O    1 
HETATM 6858 O  O    B HOH   F 5 .   ? 8.173  7.348   2.373   0.30 29.76 ?  522 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 16.382 -21.145 18.742  1.00 40.58 ?  523 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 15.795 -12.174 27.392  1.00 45.57 ?  524 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 14.734 -22.730 19.843  1.00 34.96 ?  525 HOH   A O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 29.834 -22.445 5.511   1.00 20.65 ?  201 HOH   B O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 41.720 -36.016 -17.123 1.00 33.27 ?  202 HOH   B O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 27.716 -29.188 -1.831  1.00 37.00 ?  203 HOH   B O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 59.156 -18.696 6.853   1.00 36.64 ?  204 HOH   B O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 27.896 -41.833 -15.141 1.00 37.17 ?  205 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 38.000 -39.454 -0.153  1.00 39.46 ?  206 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 48.067 -6.911  15.573  1.00 33.27 ?  207 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 49.413 -22.704 -19.755 1.00 50.40 ?  208 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 30.949 -28.762 4.389   1.00 28.43 ?  209 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 41.379 -7.753  5.470   1.00 40.04 ?  210 HOH   B O    1 
HETATM 6872 O  O    . HOH   G 5 .   ? 47.442 -7.406  -3.904  1.00 38.33 ?  211 HOH   B O    1 
HETATM 6873 O  O    . HOH   G 5 .   ? 54.520 -9.403  -8.695  1.00 19.56 ?  212 HOH   B O    1 
HETATM 6874 O  O    . HOH   G 5 .   ? 52.979 -13.520 -20.310 1.00 35.58 ?  213 HOH   B O    1 
HETATM 6875 O  O    . HOH   G 5 .   ? 30.226 -41.027 -8.034  1.00 17.66 ?  214 HOH   B O    1 
HETATM 6876 O  O    . HOH   G 5 .   ? 56.698 -30.754 -7.756  1.00 32.74 ?  215 HOH   B O    1 
HETATM 6877 O  O    . HOH   G 5 .   ? 56.367 -19.733 7.314   1.00 32.50 ?  216 HOH   B O    1 
HETATM 6878 O  O    . HOH   G 5 .   ? 50.196 -3.400  7.155   1.00 38.30 ?  217 HOH   B O    1 
HETATM 6879 O  O    . HOH   G 5 .   ? 58.235 -12.918 8.435   1.00 33.61 ?  218 HOH   B O    1 
HETATM 6880 O  O    . HOH   G 5 .   ? 57.711 -24.535 5.028   1.00 36.46 ?  219 HOH   B O    1 
HETATM 6881 O  O    . HOH   G 5 .   ? 29.911 -26.287 4.049   1.00 28.81 ?  220 HOH   B O    1 
HETATM 6882 O  O    . HOH   G 5 .   ? 37.072 -19.879 -18.091 1.00 38.92 ?  221 HOH   B O    1 
HETATM 6883 O  O    . HOH   G 5 .   ? 44.471 -7.187  2.069   1.00 33.95 ?  222 HOH   B O    1 
HETATM 6884 O  O    . HOH   G 5 .   ? 57.166 -26.884 -7.626  1.00 39.94 ?  223 HOH   B O    1 
HETATM 6885 O  O    . HOH   G 5 .   ? 55.446 -16.571 -14.313 1.00 34.85 ?  224 HOH   B O    1 
HETATM 6886 O  O    . HOH   G 5 .   ? 34.888 -24.650 13.819  1.00 38.06 ?  225 HOH   B O    1 
HETATM 6887 O  O    . HOH   G 5 .   ? 50.768 -6.105  0.167   1.00 26.60 ?  226 HOH   B O    1 
HETATM 6888 O  O    . HOH   G 5 .   ? 57.421 -16.270 -12.194 1.00 19.18 ?  227 HOH   B O    1 
HETATM 6889 O  O    . HOH   G 5 .   ? 41.521 -39.203 -14.834 1.00 23.50 ?  228 HOH   B O    1 
HETATM 6890 O  O    . HOH   G 5 .   ? 36.069 -43.397 -8.438  1.00 35.46 ?  229 HOH   B O    1 
HETATM 6891 O  O    . HOH   G 5 .   ? 51.689 -6.468  4.379   1.00 20.19 ?  230 HOH   B O    1 
HETATM 6892 O  O    . HOH   G 5 .   ? 34.550 -36.402 -7.146  1.00 18.71 ?  231 HOH   B O    1 
HETATM 6893 O  O    . HOH   G 5 .   ? 46.362 -1.567  13.205  1.00 27.79 ?  232 HOH   B O    1 
HETATM 6894 O  O    . HOH   G 5 .   ? 48.604 -36.525 -15.462 1.00 44.69 ?  233 HOH   B O    1 
HETATM 6895 O  O    . HOH   G 5 .   ? 41.368 -9.627  13.061  1.00 22.75 ?  234 HOH   B O    1 
HETATM 6896 O  O    . HOH   G 5 .   ? 25.426 -25.933 -1.286  1.00 33.36 ?  235 HOH   B O    1 
HETATM 6897 O  O    . HOH   G 5 .   ? 32.820 -43.822 -11.270 1.00 20.74 ?  236 HOH   B O    1 
HETATM 6898 O  O    . HOH   G 5 .   ? 44.921 -43.603 -10.477 1.00 28.74 ?  237 HOH   B O    1 
HETATM 6899 O  O    . HOH   G 5 .   ? 45.119 -35.002 6.855   1.00 44.28 ?  238 HOH   B O    1 
HETATM 6900 O  O    . HOH   G 5 .   ? 29.810 -34.162 -0.408  1.00 35.47 ?  239 HOH   B O    1 
HETATM 6901 O  O    . HOH   G 5 .   ? 40.644 -16.069 14.123  1.00 23.78 ?  240 HOH   B O    1 
HETATM 6902 O  O    . HOH   G 5 .   ? 35.114 -7.997  -3.010  1.00 17.69 ?  241 HOH   B O    1 
HETATM 6903 O  O    . HOH   G 5 .   ? 44.518 -27.760 -0.671  1.00 22.79 ?  242 HOH   B O    1 
HETATM 6904 O  O    . HOH   G 5 .   ? 39.312 -10.883 6.139   1.00 26.41 ?  243 HOH   B O    1 
HETATM 6905 O  O    . HOH   G 5 .   ? 42.575 -25.380 2.678   1.00 15.78 ?  244 HOH   B O    1 
HETATM 6906 O  O    . HOH   G 5 .   ? 50.747 -12.982 -0.452  1.00 12.25 ?  245 HOH   B O    1 
HETATM 6907 O  O    . HOH   G 5 .   ? 39.508 -11.120 0.352   1.00 16.87 ?  246 HOH   B O    1 
HETATM 6908 O  O    . HOH   G 5 .   ? 42.653 -22.866 3.872   1.00 12.30 ?  247 HOH   B O    1 
HETATM 6909 O  O    . HOH   G 5 .   ? 51.575 -13.858 11.016  1.00 28.34 ?  248 HOH   B O    1 
HETATM 6910 O  O    . HOH   G 5 .   ? 28.407 -19.693 -13.120 1.00 24.57 ?  249 HOH   B O    1 
HETATM 6911 O  O    . HOH   G 5 .   ? 43.061 -43.266 -8.137  1.00 30.27 ?  250 HOH   B O    1 
HETATM 6912 O  O    . HOH   G 5 .   ? 34.264 -18.442 11.434  1.00 25.16 ?  251 HOH   B O    1 
HETATM 6913 O  O    . HOH   G 5 .   ? 38.510 -11.070 -2.237  1.00 19.31 ?  252 HOH   B O    1 
HETATM 6914 O  O    . HOH   G 5 .   ? 57.649 -24.394 -3.775  1.00 21.33 ?  253 HOH   B O    1 
HETATM 6915 O  O    . HOH   G 5 .   ? 40.347 -12.772 -11.509 1.00 15.63 ?  254 HOH   B O    1 
HETATM 6916 O  O    . HOH   G 5 .   ? 48.003 -24.529 -17.763 1.00 32.03 ?  255 HOH   B O    1 
HETATM 6917 O  O    . HOH   G 5 .   ? 58.207 -10.677 -4.054  1.00 20.33 ?  256 HOH   B O    1 
HETATM 6918 O  O    . HOH   G 5 .   ? 41.882 -23.511 9.314   1.00 18.39 ?  257 HOH   B O    1 
HETATM 6919 O  O    . HOH   G 5 .   ? 27.145 -31.851 -9.922  1.00 21.35 ?  258 HOH   B O    1 
HETATM 6920 O  O    . HOH   G 5 .   ? 38.939 -11.932 12.350  1.00 35.88 ?  259 HOH   B O    1 
HETATM 6921 O  O    . HOH   G 5 .   ? 29.725 -25.226 -10.767 1.00 17.62 ?  260 HOH   B O    1 
HETATM 6922 O  O    . HOH   G 5 .   ? 49.754 -0.501  10.208  1.00 30.61 ?  261 HOH   B O    1 
HETATM 6923 O  O    . HOH   G 5 .   ? 43.202 -32.412 -17.043 1.00 24.45 ?  262 HOH   B O    1 
HETATM 6924 O  O    . HOH   G 5 .   ? 30.543 -42.242 -10.563 1.00 31.13 ?  263 HOH   B O    1 
HETATM 6925 O  O    . HOH   G 5 .   ? 50.976 -39.985 -8.182  1.00 35.85 ?  264 HOH   B O    1 
HETATM 6926 O  O    . HOH   G 5 .   ? 30.867 -15.729 2.697   1.00 14.00 ?  265 HOH   B O    1 
HETATM 6927 O  O    . HOH   G 5 .   ? 56.161 -23.572 -14.710 1.00 27.93 ?  266 HOH   B O    1 
HETATM 6928 O  O    . HOH   G 5 .   ? 48.037 -22.777 5.849   1.00 17.62 ?  267 HOH   B O    1 
HETATM 6929 O  O    . HOH   G 5 .   ? 57.503 -9.226  1.430   1.00 19.91 ?  268 HOH   B O    1 
HETATM 6930 O  O    . HOH   G 5 .   ? 43.389 -15.795 -12.170 1.00 14.88 ?  269 HOH   B O    1 
HETATM 6931 O  O    . HOH   G 5 .   ? 42.345 -9.921  9.383   1.00 21.00 ?  270 HOH   B O    1 
HETATM 6932 O  O    . HOH   G 5 .   ? 42.386 -34.722 3.786   1.00 27.36 ?  271 HOH   B O    1 
HETATM 6933 O  O    . HOH   G 5 .   ? 31.826 -17.914 -14.503 1.00 31.49 ?  272 HOH   B O    1 
HETATM 6934 O  O    . HOH   G 5 .   ? 28.473 -30.890 -14.688 1.00 30.88 ?  273 HOH   B O    1 
HETATM 6935 O  O    . HOH   G 5 .   ? 28.271 -34.377 -9.382  1.00 19.22 ?  274 HOH   B O    1 
HETATM 6936 O  O    . HOH   G 5 .   ? 49.327 -28.710 -6.852  1.00 15.89 ?  275 HOH   B O    1 
HETATM 6937 O  O    . HOH   G 5 .   ? 46.641 -31.266 -4.760  1.00 25.32 ?  276 HOH   B O    1 
HETATM 6938 O  O    . HOH   G 5 .   ? 46.906 -29.547 9.822   1.00 32.56 ?  277 HOH   B O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 56.952 -8.636  8.453   1.00 19.57 ?  278 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 34.960 -33.370 -19.153 1.00 35.18 ?  279 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 34.480 -12.775 2.637   1.00 24.84 ?  280 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 59.779 -15.298 8.149   1.00 32.38 ?  281 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 27.964 -22.904 -7.967  1.00 18.16 ?  282 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 41.194 -5.512  11.535  1.00 44.86 ?  283 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 27.596 -26.705 -15.614 1.00 32.73 ?  284 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 48.416 -25.057 3.130   1.00 14.02 ?  285 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 42.913 -20.305 -20.722 1.00 38.29 ?  286 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 57.138 -12.082 12.393  1.00 36.52 ?  287 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 48.717 -20.024 5.969   1.00 14.47 ?  288 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 33.529 -15.306 -13.913 1.00 21.07 ?  289 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 52.554 -10.372 13.009  1.00 22.32 ?  290 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 36.851 -12.778 -1.489  1.00 27.02 ?  291 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 49.990 -24.651 5.836   1.00 33.09 ?  292 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 47.093 -33.984 -4.578  1.00 18.42 ?  293 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 51.232 -37.612 -9.569  1.00 27.31 ?  294 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 45.308 -33.415 -15.896 1.00 24.68 ?  295 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 37.513 -18.067 13.121  1.00 31.61 ?  296 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 44.646 -27.462 2.033   1.00 15.79 ?  297 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 42.715 -12.276 -18.481 1.00 29.97 ?  298 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 45.914 -40.409 -3.512  1.00 29.54 ?  299 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 44.056 -29.366 -4.644  1.00 24.11 ?  300 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 53.036 -16.023 -12.724 1.00 27.05 ?  301 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 42.364 -9.884  -14.894 1.00 39.53 ?  302 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 35.069 -33.563 4.565   1.00 29.39 ?  303 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 52.622 -35.647 -8.636  1.00 30.20 ?  304 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 52.510 -29.283 -13.019 1.00 25.87 ?  305 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 40.271 -10.856 -9.540  1.00 17.41 ?  306 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 51.716 -5.990  -7.880  1.00 47.64 ?  307 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 51.358 -33.042 -10.751 1.00 42.24 ?  308 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 53.493 -30.203 4.554   1.00 19.92 ?  309 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 62.718 -13.572 4.769   1.00 27.05 ?  310 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 25.956 -21.480 -3.495  1.00 17.12 ?  311 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 32.817 -34.596 -5.846  1.00 17.72 ?  312 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 37.868 -10.256 -10.734 1.00 17.58 ?  313 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 41.764 -8.050  1.358   1.00 24.47 ?  314 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 37.118 -30.636 -20.964 1.00 31.68 ?  315 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 62.878 -20.172 -0.782  1.00 37.60 ?  316 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 43.221 -21.449 10.702  1.00 16.96 ?  317 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 53.666 -12.593 -22.194 1.00 33.41 ?  318 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 26.348 -21.056 -6.229  1.00 16.98 ?  319 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 38.351 -12.709 7.939   1.00 19.43 ?  320 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 37.271 -35.677 7.263   1.00 34.17 ?  321 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 38.418 -9.378  -13.269 1.00 27.36 ?  322 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 44.644 -24.599 9.598   1.00 20.90 ?  323 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 36.734 -12.415 4.300   1.00 18.54 ?  324 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 48.624 -12.025 -14.122 1.00 26.62 ?  325 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 59.925 -17.219 -10.511 1.00 34.73 ?  326 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 43.485 -15.389 18.178  1.00 29.15 ?  327 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 44.157 -1.764  7.621   1.00 47.20 ?  328 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 57.642 -22.052 3.272   1.00 29.24 ?  329 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 48.108 -32.659 -16.644 1.00 43.88 ?  330 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 43.138 -34.636 0.147   1.00 20.91 ?  331 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 47.196 -24.497 8.204   1.00 27.72 ?  332 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 33.618 -31.196 11.074  1.00 35.49 ?  333 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 27.917 -14.785 -9.466  1.00 35.96 ?  334 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 41.210 -24.495 15.879  1.00 44.24 ?  335 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 45.709 -36.312 -16.073 1.00 36.77 ?  336 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 47.485 -27.445 2.035   1.00 15.46 ?  337 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 42.839 -43.514 -14.321 1.00 43.05 ?  338 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 46.850 -19.887 12.307  1.00 29.52 ?  339 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 37.052 -15.129 -16.492 1.00 41.90 ?  340 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 38.468 -12.239 -16.242 1.00 43.88 ?  341 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 37.091 -45.218 -9.705  1.00 35.80 ?  342 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 28.889 -42.952 -12.318 1.00 37.76 ?  343 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 39.528 -23.666 -20.362 1.00 35.57 ?  344 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 33.019 -14.690 1.078   1.00 19.60 ?  345 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 34.531 -10.331 7.679   1.00 24.08 ?  346 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 39.832 -44.289 -11.158 1.00 41.02 ?  347 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 38.578 -22.370 15.032  1.00 41.03 ?  348 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 62.540 -20.041 -4.782  1.00 45.43 ?  349 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 33.697 -9.612  -8.854  1.00 32.77 ?  350 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 27.770 -26.594 -0.543  1.00 30.64 ?  351 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 40.435 -43.523 -9.043  1.00 26.45 ?  352 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 55.658 -8.256  10.821  1.00 24.53 ?  353 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 44.171 -37.302 -17.758 1.00 34.61 ?  354 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 56.602 -7.286  3.104   1.00 27.48 ?  355 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 36.050 -8.569  -9.739  1.00 35.79 ?  356 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 23.192 -23.647 6.846   1.00 34.30 ?  357 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 34.076 -7.802  11.453  1.00 39.44 ?  358 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 61.504 -19.930 1.742   1.00 37.42 ?  359 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 56.932 -21.583 -16.330 1.00 39.75 ?  360 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 40.245 -8.822  9.884   1.00 38.32 ?  361 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 27.164 -25.967 -11.366 1.00 34.17 ?  362 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 43.214 -12.699 -21.171 1.00 41.12 ?  363 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 40.235 -11.360 -13.954 1.00 32.39 ?  364 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 54.217 -5.728  2.985   1.00 36.59 ?  365 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 32.555 -23.610 14.086  1.00 39.28 ?  366 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 58.932 -10.443 9.231   1.00 38.46 ?  367 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 48.376 -26.471 8.829   1.00 39.30 ?  368 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 36.159 -8.641  8.977   1.00 38.07 ?  369 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 39.857 -7.032  7.841   1.00 39.24 ?  370 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 41.797 -10.056 -17.420 1.00 58.01 ?  371 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 56.049 -7.793  -0.638  1.00 34.06 ?  372 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 52.048 -12.957 13.387  1.00 28.89 ?  373 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 63.018 -12.346 6.954   1.00 37.87 ?  374 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 41.855 -6.774  -4.882  1.00 46.12 ?  375 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 38.020 -10.554 10.070  1.00 28.64 ?  376 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 36.541 -22.858 13.303  1.00 28.86 ?  377 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 42.660 -17.103 -23.126 1.00 44.43 ?  378 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 44.105 -5.607  -3.509  1.00 43.36 ?  379 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 40.141 -7.674  3.197   1.00 37.72 ?  380 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 39.672 -14.046 15.721  1.00 48.05 ?  381 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 52.878 -29.875 7.246   1.00 23.97 ?  382 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 60.517 -22.207 2.859   1.00 46.89 ?  383 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 25.840 -18.900 -11.859 1.00 37.80 ?  384 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 46.812 -5.373  2.914   1.00 38.92 ?  385 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 35.263 -20.304 13.284  1.00 32.93 ?  386 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 40.953 -9.768  15.825  1.00 46.44 ?  387 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 23.948 -20.941 -7.645  1.00 29.10 ?  388 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 35.388 -33.721 7.385   1.00 41.07 ?  389 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 23.193 -23.797 1.585   1.00 31.56 ?  390 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 40.736 -6.625  -0.871  1.00 25.25 ?  391 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 44.080 -31.717 -3.747  1.00 37.64 ?  392 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 27.964 -27.094 2.251   1.00 31.26 ?  393 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 26.620 -28.003 -13.428 1.00 36.13 ?  394 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 50.649 -30.844 8.722   1.00 29.63 ?  395 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 24.626 -20.654 -10.499 1.00 37.46 ?  396 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 34.365 -33.487 9.655   1.00 36.03 ?  397 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 26.858 -30.692 -12.584 1.00 29.48 ?  398 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 57.738 -6.567  -2.334  1.00 34.72 ?  399 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 45.749 -20.139 15.214  1.00 48.24 ?  400 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 40.875 -11.786 -22.289 1.00 38.89 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . VAL   A 3   ? 0.6585 0.6737 0.7635 0.0039  -0.0493 0.1129  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6567 0.6714 0.7493 0.0018  -0.0465 0.1126  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6325 0.6516 0.7034 -0.0078 -0.0446 0.1135  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6373 0.6565 0.7198 -0.0056 -0.0491 0.1180  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6749 0.6859 0.7701 0.0069  -0.0461 0.1101  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6817 0.6901 0.7721 0.0094  -0.0469 0.1093  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6809 0.6910 0.7732 0.0083  -0.0462 0.1094  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.5992 0.6226 0.6273 -0.0200 -0.0374 0.1081  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5602 0.5888 0.5444 -0.0330 -0.0298 0.1005  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5001 0.5441 0.4836 -0.0470 -0.0135 0.0626  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5014 0.5467 0.4795 -0.0473 -0.0166 0.0658  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5753 0.5962 0.5100 -0.0324 -0.0379 0.1303  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5852 0.5999 0.4755 -0.0325 -0.0457 0.1576  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5896 0.6002 0.4637 -0.0330 -0.0512 0.1675  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5871 0.6009 0.4670 -0.0314 -0.0469 0.1700  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4637 0.5217 0.4487 -0.0612 0.0007  0.0412  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4723 0.5149 0.4558 -0.0487 -0.0077 0.0432  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4242 0.4977 0.4146 -0.0759 0.0166  0.0182  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4416 0.4839 0.4260 -0.0513 -0.0007 0.0247  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.3780 0.4607 0.3725 -0.0887 0.0314  0.0077  5   SER   A C   
35   C  C   B SER   A 5   ? 0.4054 0.4459 0.3837 -0.0531 0.0054  0.0148  5   SER   A C   
36   O  O   A SER   A 5   ? 0.3825 0.4665 0.3724 -0.0817 0.0339  -0.0017 5   SER   A O   
37   O  O   B SER   A 5   ? 0.4063 0.4477 0.3852 -0.0519 0.0044  0.0106  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4307 0.5085 0.4292 -0.0786 0.0174  0.0069  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4461 0.4897 0.4398 -0.0527 0.0001  0.0177  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4345 0.5144 0.4355 -0.0801 0.0182  0.0010  5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4483 0.4927 0.4457 -0.0536 0.0005  0.0140  5   SER   A OG  
52   N  N   A PHE   A 6   ? 0.3239 0.4163 0.3177 -0.1084 0.0443  0.0137  6   PHE   A N   
53   N  N   B PHE   A 6   ? 0.3665 0.4053 0.3336 -0.0556 0.0130  0.0126  6   PHE   A N   
54   C  CA  A PHE   A 6   ? 0.2761 0.3695 0.2618 -0.1203 0.0496  0.0294  6   PHE   A CA  
55   C  CA  B PHE   A 6   ? 0.3288 0.3635 0.2842 -0.0569 0.0198  0.0141  6   PHE   A CA  
56   C  C   A PHE   A 6   ? 0.2685 0.3610 0.2564 -0.1227 0.0603  0.0221  6   PHE   A C   
57   C  C   B PHE   A 6   ? 0.3144 0.3477 0.2704 -0.0568 0.0296  0.0115  6   PHE   A C   
58   O  O   A PHE   A 6   ? 0.2734 0.3642 0.2884 -0.1212 0.0719  0.0297  6   PHE   A O   
59   O  O   B PHE   A 6   ? 0.3148 0.3477 0.2642 -0.0601 0.0330  0.0146  6   PHE   A O   
60   C  CB  A PHE   A 6   ? 0.2501 0.3347 0.2282 -0.1155 0.0345  0.0459  6   PHE   A CB  
61   C  CB  B PHE   A 6   ? 0.3095 0.3391 0.2571 -0.0546 0.0139  0.0157  6   PHE   A CB  
62   C  CG  A PHE   A 6   ? 0.2296 0.3067 0.2007 -0.1042 0.0193  0.0472  6   PHE   A CG  
63   C  CG  B PHE   A 6   ? 0.2917 0.3169 0.2356 -0.0530 0.0089  0.0164  6   PHE   A CG  
64   C  CD1 A PHE   A 6   ? 0.2191 0.2962 0.1874 -0.0943 0.0092  0.0410  6   PHE   A CD1 
65   C  CD1 B PHE   A 6   ? 0.2838 0.3074 0.2254 -0.0518 0.0039  0.0159  6   PHE   A CD1 
66   C  CD2 A PHE   A 6   ? 0.2355 0.2991 0.2127 -0.0859 0.0182  0.0501  6   PHE   A CD2 
67   C  CD2 B PHE   A 6   ? 0.2875 0.3078 0.2316 -0.0485 0.0100  0.0176  6   PHE   A CD2 
68   C  CE1 A PHE   A 6   ? 0.2150 0.2888 0.1976 -0.0915 0.0155  0.0454  6   PHE   A CE1 
69   C  CE1 B PHE   A 6   ? 0.2797 0.3012 0.2267 -0.0514 0.0049  0.0171  6   PHE   A CE1 
70   C  CE2 A PHE   A 6   ? 0.2322 0.2932 0.2204 -0.0799 0.0154  0.0421  6   PHE   A CE2 
71   C  CE2 B PHE   A 6   ? 0.2835 0.3016 0.2296 -0.0480 0.0093  0.0169  6   PHE   A CE2 
72   C  CZ  A PHE   A 6   ? 0.2237 0.2880 0.2079 -0.0839 0.0168  0.0441  6   PHE   A CZ  
73   C  CZ  B PHE   A 6   ? 0.2808 0.2995 0.2271 -0.0485 0.0062  0.0166  6   PHE   A CZ  
92   N  N   A SER   A 7   ? 0.2534 0.3469 0.2207 -0.1223 0.0601  0.0111  7   SER   A N   
93   N  N   B SER   A 7   ? 0.2998 0.3321 0.2660 -0.0524 0.0315  0.0062  7   SER   A N   
94   C  CA  A SER   A 7   ? 0.2535 0.3379 0.2224 -0.1063 0.0464  -0.0094 7   SER   A CA  
95   C  CA  B SER   A 7   ? 0.2903 0.3196 0.2710 -0.0446 0.0308  -0.0004 7   SER   A CA  
96   C  C   A SER   A 7   ? 0.2339 0.2991 0.1895 -0.1029 0.0527  -0.0133 7   SER   A C   
97   C  C   B SER   A 7   ? 0.2731 0.2977 0.2485 -0.0446 0.0379  -0.0010 7   SER   A C   
98   O  O   A SER   A 7   ? 0.2461 0.2877 0.1894 -0.1102 0.0547  -0.0164 7   SER   A O   
99   O  O   B SER   A 7   ? 0.2746 0.2962 0.2459 -0.0444 0.0349  -0.0035 7   SER   A O   
100  C  CB  A SER   A 7   ? 0.2775 0.3650 0.2529 -0.0868 0.0397  -0.0084 7   SER   A CB  
101  C  CB  B SER   A 7   ? 0.2965 0.3279 0.2926 -0.0386 0.0244  -0.0027 7   SER   A CB  
102  O  OG  A SER   A 7   ? 0.2982 0.3804 0.2802 -0.0718 0.0323  -0.0110 7   SER   A OG  
103  O  OG  B SER   A 7   ? 0.3009 0.3326 0.3094 -0.0340 0.0164  -0.0019 7   SER   A OG  
114  N  N   A GLY   A 8   ? 0.2116 0.2716 0.1844 -0.0880 0.0418  -0.0187 8   GLY   A N   
115  N  N   B GLY   A 8   ? 0.2571 0.2790 0.2255 -0.0456 0.0441  -0.0010 8   GLY   A N   
116  C  CA  A GLY   A 8   ? 0.1977 0.2459 0.1915 -0.0619 0.0387  -0.0142 8   GLY   A CA  
117  C  CA  B GLY   A 8   ? 0.2402 0.2586 0.2060 -0.0439 0.0442  -0.0014 8   GLY   A CA  
118  C  C   A GLY   A 8   ? 0.1756 0.2263 0.1785 -0.0436 0.0330  -0.0074 8   GLY   A C   
119  C  C   B GLY   A 8   ? 0.2219 0.2410 0.1820 -0.0429 0.0478  0.0007  8   GLY   A C   
120  O  O   A GLY   A 8   ? 0.1817 0.2296 0.1823 -0.0280 0.0323  -0.0199 8   GLY   A O   
121  O  O   B GLY   A 8   ? 0.2211 0.2404 0.1769 -0.0409 0.0575  -0.0019 8   GLY   A O   
128  N  N   A TYR   A 9   ? 0.1526 0.2088 0.1726 -0.0329 0.0291  0.0104  9   TYR   A N   
129  N  N   B TYR   A 9   ? 0.2036 0.2245 0.1780 -0.0384 0.0364  0.0040  9   TYR   A N   
130  C  CA  A TYR   A 9   ? 0.1410 0.1913 0.1678 -0.0306 0.0196  0.0113  9   TYR   A CA  
131  C  CA  B TYR   A 9   ? 0.1908 0.2078 0.1712 -0.0329 0.0285  0.0082  9   TYR   A CA  
132  C  C   A TYR   A 9   ? 0.1453 0.1702 0.1603 -0.0200 0.0280  0.0240  9   TYR   A C   
133  C  C   B TYR   A 9   ? 0.1866 0.1898 0.1653 -0.0253 0.0244  0.0121  9   TYR   A C   
134  O  O   A TYR   A 9   ? 0.1743 0.1825 0.1756 -0.0178 0.0198  0.0142  9   TYR   A O   
135  O  O   B TYR   A 9   ? 0.1953 0.1979 0.1800 -0.0270 0.0194  0.0178  9   TYR   A O   
136  C  CB  A TYR   A 9   ? 0.1335 0.2038 0.1795 -0.0272 0.0176  0.0038  9   TYR   A CB  
137  C  CB  B TYR   A 9   ? 0.1846 0.2118 0.1796 -0.0328 0.0231  0.0035  9   TYR   A CB  
138  C  CG  A TYR   A 9   ? 0.1398 0.2117 0.1885 -0.0193 0.0265  -0.0019 9   TYR   A CG  
139  C  CG  B TYR   A 9   ? 0.1801 0.2142 0.1795 -0.0350 0.0215  0.0055  9   TYR   A CG  
140  C  CD1 A TYR   A 9   ? 0.1461 0.2188 0.1964 -0.0323 0.0343  -0.0127 9   TYR   A CD1 
141  C  CD1 B TYR   A 9   ? 0.1813 0.2171 0.1873 -0.0417 0.0225  0.0038  9   TYR   A CD1 
142  C  CD2 A TYR   A 9   ? 0.1353 0.2062 0.1898 -0.0137 0.0163  0.0113  9   TYR   A CD2 
143  C  CD2 B TYR   A 9   ? 0.1779 0.2114 0.1708 -0.0345 0.0184  0.0080  9   TYR   A CD2 
144  C  CE1 A TYR   A 9   ? 0.1575 0.2263 0.2151 -0.0331 0.0399  -0.0220 9   TYR   A CE1 
145  C  CE1 B TYR   A 9   ? 0.1839 0.2193 0.1917 -0.0452 0.0249  0.0003  9   TYR   A CE1 
146  C  CE2 A TYR   A 9   ? 0.1391 0.2149 0.1976 -0.0145 0.0266  -0.0021 9   TYR   A CE2 
147  C  CE2 B TYR   A 9   ? 0.1801 0.2158 0.1793 -0.0345 0.0231  0.0071  9   TYR   A CE2 
148  C  CZ  A TYR   A 9   ? 0.1450 0.2283 0.2226 -0.0360 0.0463  -0.0138 9   TYR   A CZ  
149  C  CZ  B TYR   A 9   ? 0.1850 0.2206 0.1949 -0.0402 0.0335  0.0060  9   TYR   A CZ  
150  O  OH  A TYR   A 9   ? 0.1511 0.2424 0.2560 -0.0574 0.0448  -0.0144 9   TYR   A OH  
151  O  OH  B TYR   A 9   ? 0.1932 0.2270 0.2126 -0.0424 0.0430  0.0124  9   TYR   A OH  
170  N  N   A LEU   A 10  ? 0.1499 0.1505 0.1649 -0.0250 0.0160  0.0188  10  LEU   A N   
171  N  N   B LEU   A 10  ? 0.1835 0.1739 0.1592 -0.0188 0.0165  0.0046  10  LEU   A N   
172  C  CA  A LEU   A 10  ? 0.1380 0.1483 0.1564 -0.0280 0.0196  0.0268  10  LEU   A CA  
173  C  CA  B LEU   A 10  ? 0.1817 0.1659 0.1664 -0.0139 0.0101  -0.0032 10  LEU   A CA  
174  C  C   A LEU   A 10  ? 0.1331 0.1474 0.1707 -0.0256 0.0209  0.0411  10  LEU   A C   
175  C  C   B LEU   A 10  ? 0.1745 0.1596 0.1509 -0.0174 0.0062  0.0080  10  LEU   A C   
176  O  O   A LEU   A 10  ? 0.1375 0.1433 0.1946 -0.0142 0.0383  0.0420  10  LEU   A O   
177  O  O   B LEU   A 10  ? 0.1766 0.1611 0.1482 -0.0152 0.0158  0.0211  10  LEU   A O   
178  C  CB  A LEU   A 10  ? 0.1406 0.1529 0.1784 -0.0215 0.0099  0.0283  10  LEU   A CB  
179  C  CB  B LEU   A 10  ? 0.1839 0.1634 0.1773 -0.0118 0.0001  -0.0035 10  LEU   A CB  
180  C  CG  A LEU   A 10  ? 0.1666 0.1708 0.2333 -0.0075 -0.0026 0.0226  10  LEU   A CG  
181  C  CG  B LEU   A 10  ? 0.1903 0.1701 0.1931 -0.0050 -0.0157 -0.0040 10  LEU   A CG  
182  C  CD1 A LEU   A 10  ? 0.1834 0.1761 0.2637 -0.0201 0.0038  0.0160  10  LEU   A CD1 
183  C  CD1 B LEU   A 10  ? 0.1942 0.1798 0.2099 -0.0127 -0.0217 -0.0039 10  LEU   A CD1 
184  C  CD2 A LEU   A 10  ? 0.1796 0.1885 0.2513 0.0089  0.0063  0.0086  10  LEU   A CD2 
185  C  CD2 B LEU   A 10  ? 0.2011 0.1775 0.2114 0.0072  -0.0240 -0.0076 10  LEU   A CD2 
208  N  N   A LYS   A 11  ? 0.1395 0.1505 0.1783 -0.0307 0.0209  0.0358  11  LYS   A N   
209  N  N   B LYS   A 11  ? 0.1740 0.1563 0.1432 -0.0244 -0.0022 0.0077  11  LYS   A N   
210  C  CA  A LYS   A 11  ? 0.1401 0.1457 0.1894 -0.0305 0.0203  0.0340  11  LYS   A CA  
211  C  CA  B LYS   A 11  ? 0.1730 0.1482 0.1468 -0.0246 -0.0008 0.0068  11  LYS   A CA  
212  C  C   A LYS   A 11  ? 0.1337 0.1441 0.1979 -0.0237 0.0255  0.0223  11  LYS   A C   
213  C  C   B LYS   A 11  ? 0.1574 0.1310 0.1480 -0.0215 0.0077  -0.0033 11  LYS   A C   
214  O  O   A LYS   A 11  ? 0.1459 0.1694 0.2241 -0.0477 0.0314  0.0074  11  LYS   A O   
215  O  O   B LYS   A 11  ? 0.1502 0.1233 0.1590 -0.0206 0.0109  -0.0256 11  LYS   A O   
216  C  CB  A LYS   A 11  ? 0.1472 0.1486 0.1858 -0.0346 0.0114  0.0297  11  LYS   A CB  
217  C  CB  B LYS   A 11  ? 0.1836 0.1485 0.1534 -0.0260 -0.0044 0.0095  11  LYS   A CB  
218  C  CG  A LYS   A 11  ? 0.1580 0.1450 0.1969 -0.0368 0.0124  0.0386  11  LYS   A CG  
219  C  CG  B LYS   A 11  ? 0.1918 0.1506 0.1523 -0.0255 -0.0021 0.0181  11  LYS   A CG  
220  C  CD  A LYS   A 11  ? 0.1773 0.1520 0.1958 -0.0282 0.0062  0.0385  11  LYS   A CD  
221  C  CD  B LYS   A 11  ? 0.1998 0.1563 0.1530 -0.0224 0.0022  0.0226  11  LYS   A CD  
222  C  CE  A LYS   A 11  ? 0.1928 0.1548 0.1956 -0.0171 0.0119  0.0439  11  LYS   A CE  
223  C  CE  B LYS   A 11  ? 0.2024 0.1595 0.1544 -0.0198 0.0040  0.0245  11  LYS   A CE  
224  N  NZ  A LYS   A 11  ? 0.1940 0.1556 0.2068 -0.0013 0.0052  0.0418  11  LYS   A NZ  
225  N  NZ  B LYS   A 11  ? 0.2023 0.1618 0.1513 -0.0161 0.0049  0.0275  11  LYS   A NZ  
252  N  N   A LEU   A 12  ? 0.1264 0.1371 0.1984 -0.0250 0.0231  0.0190  12  LEU   A N   
253  N  N   B LEU   A 12  ? 0.1515 0.1396 0.1504 -0.0057 0.0099  -0.0036 12  LEU   A N   
254  C  CA  A LEU   A 12  ? 0.1311 0.1409 0.1820 -0.0158 0.0127  0.0234  12  LEU   A CA  
255  C  CA  B LEU   A 12  ? 0.1497 0.1496 0.1546 0.0020  0.0197  0.0054  12  LEU   A CA  
256  C  C   A LEU   A 12  ? 0.1377 0.1313 0.1810 -0.0157 0.0110  0.0263  12  LEU   A C   
257  C  C   B LEU   A 12  ? 0.1507 0.1539 0.1577 0.0030  0.0256  0.0039  12  LEU   A C   
258  O  O   A LEU   A 12  ? 0.1416 0.1338 0.1804 -0.0116 0.0174  0.0102  12  LEU   A O   
259  O  O   B LEU   A 12  ? 0.1546 0.1555 0.1496 0.0081  0.0253  -0.0011 12  LEU   A O   
260  C  CB  A LEU   A 12  ? 0.1368 0.1385 0.1803 -0.0124 0.0054  0.0239  12  LEU   A CB  
261  C  CB  B LEU   A 12  ? 0.1536 0.1617 0.1734 0.0069  0.0224  0.0134  12  LEU   A CB  
262  C  CG  A LEU   A 12  ? 0.1474 0.1516 0.1945 -0.0005 0.0211  0.0236  12  LEU   A CG  
263  C  CG  B LEU   A 12  ? 0.1554 0.1673 0.1974 0.0115  0.0301  0.0156  12  LEU   A CG  
264  C  CD1 A LEU   A 12  ? 0.1541 0.1534 0.1873 0.0118  0.0313  0.0353  12  LEU   A CD1 
265  C  CD1 B LEU   A 12  ? 0.1530 0.1736 0.2066 0.0189  0.0391  0.0184  12  LEU   A CD1 
266  C  CD2 A LEU   A 12  ? 0.1471 0.1605 0.2157 -0.0017 0.0166  0.0264  12  LEU   A CD2 
267  C  CD2 B LEU   A 12  ? 0.1565 0.1711 0.2065 0.0107  0.0302  0.0041  12  LEU   A CD2 
290  N  N   A THR   A 13  ? 0.1343 0.1289 0.1986 -0.0158 0.0089  0.0210  13  THR   A N   
291  N  N   B THR   A 13  ? 0.1468 0.1530 0.1695 -0.0010 0.0250  0.0071  13  THR   A N   
292  C  CA  A THR   A 13  ? 0.1353 0.1359 0.2002 -0.0120 0.0141  0.0200  13  THR   A CA  
293  C  CA  B THR   A 13  ? 0.1441 0.1548 0.1659 -0.0049 0.0289  0.0158  13  THR   A CA  
294  C  C   A THR   A 13  ? 0.1365 0.1389 0.2108 -0.0179 0.0060  0.0377  13  THR   A C   
295  C  C   B THR   A 13  ? 0.1523 0.1600 0.1690 -0.0112 0.0249  0.0287  13  THR   A C   
296  O  O   A THR   A 13  ? 0.1337 0.1426 0.2153 -0.0131 0.0062  0.0336  13  THR   A O   
297  O  O   B THR   A 13  ? 0.1600 0.1671 0.1709 -0.0144 0.0162  0.0355  13  THR   A O   
298  C  CB  A THR   A 13  ? 0.1422 0.1529 0.2121 -0.0055 0.0139  0.0254  13  THR   A CB  
299  C  CB  B THR   A 13  ? 0.1376 0.1579 0.1711 -0.0011 0.0351  0.0185  13  THR   A CB  
300  O  OG1 A THR   A 13  ? 0.1469 0.1449 0.2273 -0.0104 0.0022  0.0325  13  THR   A OG1 
301  O  OG1 B THR   A 13  ? 0.1227 0.1571 0.1835 -0.0078 0.0470  0.0324  13  THR   A OG1 
302  C  CG2 A THR   A 13  ? 0.1518 0.1676 0.2173 -0.0078 0.0243  0.0121  13  THR   A CG2 
303  C  CG2 B THR   A 13  ? 0.1412 0.1636 0.1739 0.0032  0.0372  0.0112  13  THR   A CG2 
318  N  N   A ASP   A 14  ? 0.1417 0.1435 0.2240 -0.0223 -0.0005 0.0508  14  ASP   A N   
319  N  N   B ASP   A 14  ? 0.1538 0.1594 0.1908 -0.0152 0.0157  0.0345  14  ASP   A N   
320  C  CA  A ASP   A 14  ? 0.1446 0.1619 0.2533 -0.0186 -0.0081 0.0676  14  ASP   A CA  
321  C  CA  B ASP   A 14  ? 0.1568 0.1640 0.2167 -0.0169 0.0057  0.0474  14  ASP   A CA  
322  C  C   A ASP   A 14  ? 0.1487 0.1651 0.2313 -0.0226 -0.0141 0.0598  14  ASP   A C   
323  C  C   B ASP   A 14  ? 0.1488 0.1581 0.2140 -0.0235 -0.0040 0.0559  14  ASP   A C   
324  O  O   A ASP   A 14  ? 0.1701 0.1769 0.2372 -0.0303 -0.0193 0.0664  14  ASP   A O   
325  O  O   B ASP   A 14  ? 0.1554 0.1589 0.2198 -0.0328 -0.0082 0.0599  14  ASP   A O   
326  C  CB  A ASP   A 14  ? 0.1588 0.1898 0.3256 -0.0228 -0.0082 0.0850  14  ASP   A CB  
327  C  CB  B ASP   A 14  ? 0.1669 0.1809 0.2546 -0.0154 -0.0017 0.0470  14  ASP   A CB  
328  C  CG  A ASP   A 14  ? 0.1805 0.2394 0.4093 -0.0244 -0.0045 0.0868  14  ASP   A CG  
329  C  CG  B ASP   A 14  ? 0.1727 0.2098 0.2899 -0.0204 -0.0029 0.0454  14  ASP   A CG  
330  O  OD1 A ASP   A 14  ? 0.1971 0.2600 0.4415 -0.0088 -0.0134 0.0897  14  ASP   A OD1 
331  O  OD1 B ASP   A 14  ? 0.1819 0.2190 0.3006 -0.0097 -0.0067 0.0537  14  ASP   A OD1 
332  O  OD2 A ASP   A 14  ? 0.1998 0.2690 0.4531 -0.0275 -0.0120 0.0689  14  ASP   A OD2 
333  O  OD2 B ASP   A 14  ? 0.1757 0.2314 0.3129 -0.0268 -0.0091 0.0341  14  ASP   A OD2 
342  N  N   . ASN   A 15  ? 0.1389 0.1502 0.2232 -0.0234 -0.0005 0.0602  15  ASN   A N   
343  C  CA  . ASN   A 15  ? 0.1429 0.1541 0.2384 -0.0196 -0.0088 0.0509  15  ASN   A CA  
344  C  C   . ASN   A 15  ? 0.1384 0.1503 0.2495 -0.0214 -0.0006 0.0477  15  ASN   A C   
345  O  O   . ASN   A 15  ? 0.1467 0.1515 0.2983 -0.0183 -0.0199 0.0523  15  ASN   A O   
346  C  CB  . ASN   A 15  ? 0.1381 0.1561 0.2280 -0.0101 -0.0028 0.0474  15  ASN   A CB  
347  C  CG  . ASN   A 15  ? 0.1439 0.1628 0.2331 -0.0081 0.0035  0.0338  15  ASN   A CG  
348  O  OD1 . ASN   A 15  ? 0.1598 0.1631 0.2555 -0.0259 -0.0039 0.0353  15  ASN   A OD1 
349  N  ND2 . ASN   A 15  ? 0.1457 0.1783 0.2171 -0.0150 0.0130  0.0315  15  ASN   A ND2 
357  N  N   A VAL   A 16  ? 0.1381 0.1444 0.2324 -0.0172 0.0063  0.0526  16  VAL   A N   
358  N  N   B VAL   A 16  ? 0.1383 0.1583 0.2157 -0.0198 0.0121  0.0488  16  VAL   A N   
359  C  CA  A VAL   A 16  ? 0.1322 0.1474 0.2273 -0.0176 0.0075  0.0469  16  VAL   A CA  
360  C  CA  B VAL   A 16  ? 0.1379 0.1652 0.1818 -0.0193 0.0223  0.0493  16  VAL   A CA  
361  C  C   A VAL   A 16  ? 0.1294 0.1440 0.2051 -0.0209 0.0021  0.0411  16  VAL   A C   
362  C  C   B VAL   A 16  ? 0.1347 0.1720 0.1673 -0.0213 0.0139  0.0448  16  VAL   A C   
363  O  O   A VAL   A 16  ? 0.1271 0.1370 0.1922 -0.0197 0.0096  0.0286  16  VAL   A O   
364  O  O   B VAL   A 16  ? 0.1314 0.1754 0.1617 -0.0175 0.0143  0.0349  16  VAL   A O   
365  C  CB  A VAL   A 16  ? 0.1410 0.1633 0.2288 0.0023  0.0185  0.0553  16  VAL   A CB  
366  C  CB  B VAL   A 16  ? 0.1450 0.1693 0.1682 -0.0069 0.0366  0.0484  16  VAL   A CB  
367  C  CG1 A VAL   A 16  ? 0.1539 0.1803 0.2354 0.0087  0.0286  0.0487  16  VAL   A CG1 
368  C  CG1 B VAL   A 16  ? 0.1527 0.1745 0.1756 0.0006  0.0386  0.0435  16  VAL   A CG1 
369  C  CG2 A VAL   A 16  ? 0.1472 0.1685 0.2432 0.0103  0.0308  0.0484  16  VAL   A CG2 
370  C  CG2 B VAL   A 16  ? 0.1472 0.1738 0.1816 -0.0039 0.0452  0.0389  16  VAL   A CG2 
389  N  N   A TYR   A 17  ? 0.1246 0.1357 0.2157 -0.0179 0.0094  0.0459  17  TYR   A N   
390  N  N   B TYR   A 17  ? 0.1326 0.1702 0.1686 -0.0211 0.0051  0.0395  17  TYR   A N   
391  C  CA  A TYR   A 17  ? 0.1303 0.1420 0.1975 -0.0204 0.0089  0.0457  17  TYR   A CA  
392  C  CA  B TYR   A 17  ? 0.1329 0.1694 0.1533 -0.0201 -0.0017 0.0388  17  TYR   A CA  
393  C  C   A TYR   A 17  ? 0.1339 0.1362 0.1989 -0.0180 0.0103  0.0282  17  TYR   A C   
394  C  C   B TYR   A 17  ? 0.1308 0.1649 0.1445 -0.0232 0.0039  0.0336  17  TYR   A C   
395  O  O   A TYR   A 17  ? 0.1330 0.1281 0.2034 -0.0149 0.0153  0.0322  17  TYR   A O   
396  O  O   B TYR   A 17  ? 0.1263 0.1655 0.1309 -0.0275 0.0042  0.0393  17  TYR   A O   
397  C  CB  A TYR   A 17  ? 0.1495 0.1515 0.1977 -0.0321 0.0039  0.0489  17  TYR   A CB  
398  C  CB  B TYR   A 17  ? 0.1428 0.1717 0.1615 -0.0170 -0.0079 0.0359  17  TYR   A CB  
399  C  CG  A TYR   A 17  ? 0.1761 0.1687 0.2120 -0.0392 -0.0123 0.0510  17  TYR   A CG  
400  C  CG  B TYR   A 17  ? 0.1557 0.1753 0.1660 -0.0121 -0.0115 0.0345  17  TYR   A CG  
401  C  CD1 A TYR   A 17  ? 0.1891 0.1779 0.2291 -0.0251 -0.0220 0.0492  17  TYR   A CD1 
402  C  CD1 B TYR   A 17  ? 0.1636 0.1739 0.1748 -0.0001 -0.0130 0.0393  17  TYR   A CD1 
403  C  CD2 A TYR   A 17  ? 0.1881 0.1702 0.2043 -0.0511 -0.0208 0.0532  17  TYR   A CD2 
404  C  CD2 B TYR   A 17  ? 0.1615 0.1793 0.1640 -0.0122 -0.0137 0.0307  17  TYR   A CD2 
405  C  CE1 A TYR   A 17  ? 0.1982 0.1771 0.2308 -0.0288 -0.0270 0.0487  17  TYR   A CE1 
406  C  CE1 B TYR   A 17  ? 0.1724 0.1756 0.1831 -0.0004 -0.0096 0.0414  17  TYR   A CE1 
407  C  CE2 A TYR   A 17  ? 0.1996 0.1698 0.2138 -0.0512 -0.0365 0.0393  17  TYR   A CE2 
408  C  CE2 B TYR   A 17  ? 0.1693 0.1794 0.1726 -0.0073 -0.0134 0.0282  17  TYR   A CE2 
409  C  CZ  A TYR   A 17  ? 0.2056 0.1667 0.2184 -0.0449 -0.0350 0.0485  17  TYR   A CZ  
410  C  CZ  B TYR   A 17  ? 0.1736 0.1781 0.1795 -0.0018 -0.0129 0.0393  17  TYR   A CZ  
411  O  OH  A TYR   A 17  ? 0.2183 0.1624 0.2307 -0.0435 -0.0320 0.0445  17  TYR   A OH  
412  O  OH  B TYR   A 17  ? 0.1769 0.1822 0.1890 0.0047  -0.0094 0.0433  17  TYR   A OH  
431  N  N   A ILE   A 18  ? 0.1394 0.1392 0.1936 -0.0156 0.0150  0.0334  18  ILE   A N   
432  N  N   B ILE   A 18  ? 0.1278 0.1564 0.1484 -0.0229 0.0162  0.0311  18  ILE   A N   
433  C  CA  A ILE   A 18  ? 0.1408 0.1372 0.1825 -0.0143 0.0182  0.0250  18  ILE   A CA  
434  C  CA  B ILE   A 18  ? 0.1233 0.1468 0.1338 -0.0162 0.0272  0.0195  18  ILE   A CA  
435  C  C   A ILE   A 18  ? 0.1481 0.1486 0.1763 -0.0261 0.0155  0.0246  18  ILE   A C   
436  C  C   B ILE   A 18  ? 0.1207 0.1567 0.1233 -0.0174 0.0196  0.0122  18  ILE   A C   
437  O  O   A ILE   A 18  ? 0.1461 0.1608 0.1716 -0.0313 0.0189  0.0244  18  ILE   A O   
438  O  O   B ILE   A 18  ? 0.1186 0.1665 0.1345 -0.0245 0.0213  0.0059  18  ILE   A O   
439  C  CB  A ILE   A 18  ? 0.1475 0.1402 0.1621 0.0019  0.0213  0.0212  18  ILE   A CB  
440  C  CB  B ILE   A 18  ? 0.1331 0.1376 0.1190 -0.0028 0.0411  0.0197  18  ILE   A CB  
441  C  CG1 A ILE   A 18  ? 0.1534 0.1425 0.1719 0.0191  0.0111  0.0241  18  ILE   A CG1 
442  C  CG1 B ILE   A 18  ? 0.1511 0.1453 0.1295 -0.0054 0.0514  0.0220  18  ILE   A CG1 
443  C  CG2 A ILE   A 18  ? 0.1494 0.1421 0.1586 0.0054  0.0202  0.0084  18  ILE   A CG2 
444  C  CG2 B ILE   A 18  ? 0.1396 0.1406 0.1225 -0.0012 0.0363  0.0166  18  ILE   A CG2 
445  C  CD1 A ILE   A 18  ? 0.1766 0.1542 0.1855 0.0290  0.0192  0.0316  18  ILE   A CD1 
446  C  CD1 B ILE   A 18  ? 0.1642 0.1555 0.1539 -0.0023 0.0539  0.0114  18  ILE   A CD1 
469  N  N   A LYS   A 19  ? 0.1489 0.1495 0.1710 -0.0256 0.0283  0.0157  19  LYS   A N   
470  N  N   B LYS   A 19  ? 0.1238 0.1608 0.1173 -0.0075 0.0260  0.0032  19  LYS   A N   
471  C  CA  A LYS   A 19  ? 0.1624 0.1598 0.1580 -0.0209 0.0300  0.0183  19  LYS   A CA  
472  C  CA  B LYS   A 19  ? 0.1398 0.1734 0.1375 -0.0036 0.0252  -0.0064 19  LYS   A CA  
473  C  C   A LYS   A 19  ? 0.1483 0.1519 0.1616 -0.0121 0.0343  0.0320  19  LYS   A C   
474  C  C   B LYS   A 19  ? 0.1487 0.1736 0.1440 0.0040  0.0217  -0.0055 19  LYS   A C   
475  O  O   A LYS   A 19  ? 0.1431 0.1477 0.1711 -0.0067 0.0242  0.0358  19  LYS   A O   
476  O  O   B LYS   A 19  ? 0.1470 0.1714 0.1365 0.0029  0.0205  -0.0044 19  LYS   A O   
477  C  CB  A LYS   A 19  ? 0.1862 0.1861 0.1611 -0.0245 0.0220  0.0111  19  LYS   A CB  
478  C  CB  B LYS   A 19  ? 0.1402 0.1861 0.1502 -0.0069 0.0282  -0.0155 19  LYS   A CB  
479  C  CG  A LYS   A 19  ? 0.2154 0.2088 0.1702 -0.0252 0.0151  0.0028  19  LYS   A CG  
480  C  CG  B LYS   A 19  ? 0.1603 0.1979 0.1593 -0.0043 0.0200  -0.0128 19  LYS   A CG  
481  C  CD  A LYS   A 19  ? 0.2392 0.2353 0.1907 -0.0303 0.0061  -0.0013 19  LYS   A CD  
482  C  CD  B LYS   A 19  ? 0.1778 0.2096 0.1672 -0.0061 0.0124  -0.0053 19  LYS   A CD  
483  C  CE  A LYS   A 19  ? 0.2564 0.2483 0.2096 -0.0429 0.0036  0.0027  19  LYS   A CE  
484  C  CE  B LYS   A 19  ? 0.1835 0.2138 0.1687 -0.0125 0.0023  -0.0011 19  LYS   A CE  
485  N  NZ  A LYS   A 19  ? 0.2672 0.2578 0.2066 -0.0554 0.0077  -0.0012 19  LYS   A NZ  
486  N  NZ  B LYS   A 19  ? 0.1887 0.2146 0.1602 -0.0192 0.0015  0.0016  19  LYS   A NZ  
513  N  N   A ASN   A 20  ? 0.1523 0.1579 0.1868 -0.0168 0.0335  0.0382  20  ASN   A N   
514  N  N   B ASN   A 20  ? 0.1644 0.1799 0.1584 0.0091  0.0207  -0.0073 20  ASN   A N   
515  C  CA  A ASN   A 20  ? 0.1665 0.1736 0.2038 0.0044  0.0540  0.0350  20  ASN   A CA  
516  C  CA  B ASN   A 20  ? 0.1793 0.1876 0.1729 0.0134  0.0145  -0.0092 20  ASN   A CA  
517  C  C   A ASN   A 20  ? 0.1911 0.1834 0.2262 -0.0096 0.0696  0.0189  20  ASN   A C   
518  C  C   B ASN   A 20  ? 0.1911 0.1899 0.1836 0.0041  0.0186  -0.0109 20  ASN   A C   
519  O  O   A ASN   A 20  ? 0.2172 0.2022 0.2475 -0.0363 0.0696  -0.0084 20  ASN   A O   
520  O  O   B ASN   A 20  ? 0.2017 0.1972 0.1781 -0.0106 0.0158  -0.0138 20  ASN   A O   
521  C  CB  A ASN   A 20  ? 0.1692 0.1874 0.2115 0.0237  0.0548  0.0544  20  ASN   A CB  
522  C  CB  B ASN   A 20  ? 0.1892 0.1963 0.1777 0.0258  0.0136  -0.0079 20  ASN   A CB  
523  C  CG  A ASN   A 20  ? 0.1838 0.1965 0.2360 0.0426  0.0591  0.0614  20  ASN   A CG  
524  C  CG  B ASN   A 20  ? 0.2031 0.2022 0.1911 0.0325  0.0168  -0.0097 20  ASN   A CG  
525  O  OD1 A ASN   A 20  ? 0.2195 0.2064 0.2754 0.0610  0.0715  0.0534  20  ASN   A OD1 
526  O  OD1 B ASN   A 20  ? 0.2193 0.2110 0.2008 0.0315  0.0039  -0.0078 20  ASN   A OD1 
527  N  ND2 A ASN   A 20  ? 0.1934 0.1995 0.2449 0.0435  0.0534  0.0771  20  ASN   A ND2 
528  N  ND2 B ASN   A 20  ? 0.2049 0.1977 0.1893 0.0402  0.0270  -0.0209 20  ASN   A ND2 
541  N  N   A ALA   A 21  ? 0.1908 0.1800 0.2377 -0.0003 0.0620  0.0215  21  ALA   A N   
542  N  N   B ALA   A 21  ? 0.1942 0.1864 0.1999 0.0050  0.0206  -0.0051 21  ALA   A N   
543  C  CA  A ALA   A 21  ? 0.1992 0.1831 0.2450 -0.0069 0.0524  0.0301  21  ALA   A CA  
544  C  CA  B ALA   A 21  ? 0.1978 0.1844 0.2062 -0.0020 0.0318  0.0044  21  ALA   A CA  
545  C  C   A ALA   A 21  ? 0.1818 0.1838 0.2468 -0.0059 0.0468  0.0491  21  ALA   A C   
546  C  C   B ALA   A 21  ? 0.1881 0.1784 0.2076 -0.0004 0.0505  0.0181  21  ALA   A C   
547  O  O   A ALA   A 21  ? 0.1743 0.1867 0.2447 0.0130  0.0341  0.0628  21  ALA   A O   
548  O  O   B ALA   A 21  ? 0.1867 0.1739 0.2236 0.0132  0.0519  0.0147  21  ALA   A O   
549  C  CB  A ALA   A 21  ? 0.2212 0.1845 0.2494 -0.0186 0.0494  0.0307  21  ALA   A CB  
550  C  CB  B ALA   A 21  ? 0.2094 0.1869 0.2218 -0.0089 0.0268  0.0042  21  ALA   A CB  
561  N  N   A ASP   A 22  ? 0.1754 0.1788 0.2611 -0.0109 0.0427  0.0466  22  ASP   A N   
562  N  N   B ASP   A 22  ? 0.1824 0.1738 0.2008 -0.0067 0.0597  0.0309  22  ASP   A N   
563  C  CA  A ASP   A 22  ? 0.1757 0.1839 0.2522 -0.0074 0.0375  0.0379  22  ASP   A CA  
564  C  CA  B ASP   A 22  ? 0.1798 0.1716 0.1984 -0.0051 0.0594  0.0357  22  ASP   A CA  
565  C  C   A ASP   A 22  ? 0.1703 0.1887 0.2081 -0.0033 0.0392  0.0285  22  ASP   A C   
566  C  C   B ASP   A 22  ? 0.1633 0.1725 0.1732 -0.0141 0.0610  0.0271  22  ASP   A C   
567  O  O   A ASP   A 22  ? 0.1787 0.1987 0.2191 -0.0027 0.0352  0.0196  22  ASP   A O   
568  O  O   B ASP   A 22  ? 0.1576 0.1766 0.1705 -0.0169 0.0603  0.0046  22  ASP   A O   
569  C  CB  A ASP   A 22  ? 0.1892 0.1835 0.3042 -0.0106 0.0263  0.0344  22  ASP   A CB  
570  C  CB  B ASP   A 22  ? 0.1946 0.1720 0.2272 0.0061  0.0589  0.0342  22  ASP   A CB  
571  C  CG  A ASP   A 22  ? 0.2093 0.1931 0.3586 -0.0074 0.0007  0.0434  22  ASP   A CG  
572  C  CG  B ASP   A 22  ? 0.2038 0.1711 0.2364 0.0166  0.0614  0.0356  22  ASP   A CG  
573  O  OD1 A ASP   A 22  ? 0.2068 0.1992 0.3860 -0.0163 -0.0152 0.0624  22  ASP   A OD1 
574  O  OD1 B ASP   A 22  ? 0.2007 0.1656 0.2253 0.0195  0.0644  0.0332  22  ASP   A OD1 
575  O  OD2 A ASP   A 22  ? 0.2361 0.2038 0.3891 -0.0039 0.0043  0.0307  22  ASP   A OD2 
576  O  OD2 B ASP   A 22  ? 0.2147 0.1763 0.2602 0.0178  0.0678  0.0329  22  ASP   A OD2 
585  N  N   A ILE   A 23  ? 0.1706 0.1839 0.1978 0.0007  0.0393  0.0188  23  ILE   A N   
586  N  N   B ILE   A 23  ? 0.1582 0.1696 0.1711 -0.0183 0.0503  0.0257  23  ILE   A N   
587  C  CA  A ILE   A 23  ? 0.1703 0.1776 0.1859 -0.0040 0.0331  0.0193  23  ILE   A CA  
588  C  CA  B ILE   A 23  ? 0.1525 0.1714 0.1567 -0.0219 0.0357  0.0211  23  ILE   A CA  
589  C  C   A ILE   A 23  ? 0.1699 0.1858 0.1846 -0.0054 0.0452  0.0216  23  ILE   A C   
590  C  C   B ILE   A 23  ? 0.1584 0.1794 0.1588 -0.0310 0.0354  0.0058  23  ILE   A C   
591  O  O   A ILE   A 23  ? 0.1794 0.1958 0.1926 -0.0033 0.0373  0.0112  23  ILE   A O   
592  O  O   B ILE   A 23  ? 0.1588 0.1791 0.1645 -0.0286 0.0270  -0.0071 23  ILE   A O   
593  C  CB  A ILE   A 23  ? 0.1787 0.1730 0.1682 0.0010  0.0294  0.0138  23  ILE   A CB  
594  C  CB  B ILE   A 23  ? 0.1505 0.1681 0.1486 -0.0111 0.0221  0.0242  23  ILE   A CB  
595  C  CG1 A ILE   A 23  ? 0.1798 0.1708 0.1739 -0.0003 0.0214  0.0112  23  ILE   A CG1 
596  C  CG1 B ILE   A 23  ? 0.1524 0.1661 0.1382 -0.0148 0.0112  0.0153  23  ILE   A CG1 
597  C  CG2 A ILE   A 23  ? 0.1846 0.1771 0.1566 0.0020  0.0304  0.0202  23  ILE   A CG2 
598  C  CG2 B ILE   A 23  ? 0.1481 0.1639 0.1458 -0.0009 0.0193  0.0231  23  ILE   A CG2 
599  C  CD1 A ILE   A 23  ? 0.1810 0.1745 0.1772 -0.0042 0.0093  0.0037  23  ILE   A CD1 
600  C  CD1 B ILE   A 23  ? 0.1485 0.1642 0.1331 -0.0137 -0.0001 0.0127  23  ILE   A CD1 
623  N  N   A VAL   A 24  ? 0.1710 0.1887 0.1917 -0.0121 0.0381  0.0165  24  VAL   A N   
624  N  N   B VAL   A 24  ? 0.1676 0.1855 0.1713 -0.0404 0.0298  0.0010  24  VAL   A N   
625  C  CA  A VAL   A 24  ? 0.1910 0.1987 0.2105 -0.0177 0.0341  0.0050  24  VAL   A CA  
626  C  CA  B VAL   A 24  ? 0.1869 0.1930 0.1855 -0.0433 0.0294  -0.0020 24  VAL   A CA  
627  C  C   A VAL   A 24  ? 0.1901 0.2144 0.2078 -0.0286 0.0328  -0.0019 24  VAL   A C   
628  C  C   B VAL   A 24  ? 0.1952 0.2089 0.1988 -0.0419 0.0274  -0.0098 24  VAL   A C   
629  O  O   A VAL   A 24  ? 0.2021 0.2164 0.2077 -0.0286 0.0386  -0.0013 24  VAL   A O   
630  O  O   B VAL   A 24  ? 0.2061 0.2136 0.2126 -0.0386 0.0255  -0.0076 24  VAL   A O   
631  C  CB  A VAL   A 24  ? 0.2046 0.2041 0.2290 -0.0151 0.0405  0.0068  24  VAL   A CB  
632  C  CB  B VAL   A 24  ? 0.1949 0.1903 0.1943 -0.0452 0.0286  -0.0002 24  VAL   A CB  
633  C  CG1 A VAL   A 24  ? 0.2127 0.2157 0.2415 -0.0082 0.0481  -0.0014 24  VAL   A CG1 
634  C  CG1 B VAL   A 24  ? 0.2026 0.1948 0.2074 -0.0402 0.0305  0.0003  24  VAL   A CG1 
635  C  CG2 A VAL   A 24  ? 0.2176 0.2109 0.2420 -0.0149 0.0432  0.0197  24  VAL   A CG2 
636  C  CG2 B VAL   A 24  ? 0.1963 0.1855 0.1899 -0.0512 0.0243  -0.0040 24  VAL   A CG2 
655  N  N   A GLU   A 25  ? 0.1911 0.2396 0.2129 -0.0335 0.0416  -0.0138 25  GLU   A N   
656  N  N   B GLU   A 25  ? 0.1959 0.2232 0.2041 -0.0415 0.0352  -0.0180 25  GLU   A N   
657  C  CA  A GLU   A 25  ? 0.2100 0.2707 0.2119 -0.0263 0.0542  -0.0193 25  GLU   A CA  
658  C  CA  B GLU   A 25  ? 0.2048 0.2372 0.2141 -0.0447 0.0344  -0.0176 25  GLU   A CA  
659  C  C   A GLU   A 25  ? 0.1994 0.2756 0.1745 -0.0368 0.0605  -0.0189 25  GLU   A C   
660  C  C   B GLU   A 25  ? 0.2092 0.2432 0.2095 -0.0397 0.0415  -0.0160 25  GLU   A C   
661  O  O   A GLU   A 25  ? 0.2053 0.2848 0.1877 -0.0382 0.0523  -0.0206 25  GLU   A O   
662  O  O   B GLU   A 25  ? 0.2135 0.2473 0.2139 -0.0382 0.0440  -0.0208 25  GLU   A O   
663  C  CB  A GLU   A 25  ? 0.2368 0.2990 0.2532 -0.0196 0.0557  -0.0184 25  GLU   A CB  
664  C  CB  B GLU   A 25  ? 0.2121 0.2453 0.2406 -0.0485 0.0344  -0.0173 25  GLU   A CB  
665  C  CG  A GLU   A 25  ? 0.2682 0.3251 0.3146 -0.0201 0.0344  -0.0225 25  GLU   A CG  
666  C  CG  B GLU   A 25  ? 0.2277 0.2564 0.2841 -0.0503 0.0268  -0.0195 25  GLU   A CG  
667  C  CD  A GLU   A 25  ? 0.2889 0.3482 0.3633 -0.0193 0.0151  -0.0216 25  GLU   A CD  
668  C  CD  B GLU   A 25  ? 0.2384 0.2681 0.3223 -0.0514 0.0153  -0.0190 25  GLU   A CD  
669  O  OE1 A GLU   A 25  ? 0.3002 0.3604 0.3720 -0.0164 0.0010  -0.0254 25  GLU   A OE1 
670  O  OE1 B GLU   A 25  ? 0.2442 0.2739 0.3415 -0.0530 0.0089  -0.0199 25  GLU   A OE1 
671  O  OE2 A GLU   A 25  ? 0.2936 0.3549 0.3936 -0.0197 0.0076  -0.0261 25  GLU   A OE2 
672  O  OE2 B GLU   A 25  ? 0.2419 0.2737 0.3384 -0.0486 0.0113  -0.0160 25  GLU   A OE2 
685  N  N   A GLU   A 26  ? 0.1899 0.2719 0.1830 -0.0521 0.0597  -0.0216 26  GLU   A N   
686  N  N   B GLU   A 26  ? 0.2086 0.2419 0.2004 -0.0396 0.0504  -0.0145 26  GLU   A N   
687  C  CA  A GLU   A 26  ? 0.2005 0.2761 0.1723 -0.0630 0.0577  -0.0147 26  GLU   A CA  
688  C  CA  B GLU   A 26  ? 0.2170 0.2406 0.2037 -0.0374 0.0504  -0.0093 26  GLU   A CA  
689  C  C   A GLU   A 26  ? 0.2042 0.2583 0.1581 -0.0680 0.0489  -0.0020 26  GLU   A C   
690  C  C   B GLU   A 26  ? 0.2145 0.2387 0.1895 -0.0284 0.0465  0.0001  26  GLU   A C   
691  O  O   A GLU   A 26  ? 0.2172 0.2615 0.1682 -0.0763 0.0439  0.0060  26  GLU   A O   
692  O  O   B GLU   A 26  ? 0.2176 0.2406 0.1811 -0.0326 0.0481  0.0034  26  GLU   A O   
693  C  CB  A GLU   A 26  ? 0.2191 0.2904 0.1982 -0.0700 0.0638  -0.0105 26  GLU   A CB  
694  C  CB  B GLU   A 26  ? 0.2291 0.2360 0.2272 -0.0498 0.0526  -0.0083 26  GLU   A CB  
695  C  CG  A GLU   A 26  ? 0.2482 0.3156 0.2835 -0.0711 0.0576  -0.0172 26  GLU   A CG  
696  C  CG  B GLU   A 26  ? 0.2373 0.2289 0.2434 -0.0637 0.0736  -0.0121 26  GLU   A CG  
697  C  CD  A GLU   A 26  ? 0.2644 0.3355 0.3357 -0.0752 0.0645  -0.0163 26  GLU   A CD  
698  C  CD  B GLU   A 26  ? 0.2396 0.2179 0.2464 -0.0848 0.1004  -0.0133 26  GLU   A CD  
699  O  OE1 A GLU   A 26  ? 0.2673 0.3526 0.3422 -0.0699 0.0707  -0.0283 26  GLU   A OE1 
700  O  OE1 B GLU   A 26  ? 0.2339 0.2124 0.2493 -0.0984 0.1113  -0.0368 26  GLU   A OE1 
701  O  OE2 A GLU   A 26  ? 0.2799 0.3384 0.3737 -0.0815 0.0565  -0.0143 26  GLU   A OE2 
702  O  OE2 B GLU   A 26  ? 0.2427 0.2171 0.2285 -0.0805 0.1146  -0.0024 26  GLU   A OE2 
715  N  N   A ALA   A 27  ? 0.1884 0.2404 0.1529 -0.0691 0.0497  0.0039  27  ALA   A N   
716  N  N   B ALA   A 27  ? 0.2067 0.2350 0.1818 -0.0161 0.0421  0.0080  27  ALA   A N   
717  C  CA  A ALA   A 27  ? 0.1948 0.2433 0.1518 -0.0661 0.0440  0.0037  27  ALA   A CA  
718  C  CA  B ALA   A 27  ? 0.2088 0.2387 0.1803 -0.0057 0.0338  0.0128  27  ALA   A CA  
719  C  C   A ALA   A 27  ? 0.2223 0.2540 0.1639 -0.0758 0.0416  -0.0077 27  ALA   A C   
720  C  C   B ALA   A 27  ? 0.2197 0.2482 0.1858 -0.0022 0.0309  0.0129  27  ALA   A C   
721  O  O   A ALA   A 27  ? 0.2304 0.2493 0.1711 -0.0801 0.0289  -0.0056 27  ALA   A O   
722  O  O   B ALA   A 27  ? 0.2193 0.2468 0.1915 -0.0031 0.0268  0.0148  27  ALA   A O   
723  C  CB  A ALA   A 27  ? 0.1825 0.2352 0.1604 -0.0656 0.0324  0.0013  27  ALA   A CB  
724  C  CB  B ALA   A 27  ? 0.2040 0.2353 0.1758 -0.0056 0.0306  0.0138  27  ALA   A CB  
735  N  N   A LYS   A 28  ? 0.2561 0.2780 0.1802 -0.0724 0.0331  -0.0366 28  LYS   A N   
736  N  N   B LYS   A 28  ? 0.2380 0.2604 0.1985 0.0012  0.0266  0.0060  28  LYS   A N   
737  C  CA  A LYS   A 28  ? 0.2915 0.3088 0.2142 -0.0678 0.0372  -0.0510 28  LYS   A CA  
738  C  CA  B LYS   A 28  ? 0.2572 0.2787 0.2218 0.0044  0.0209  -0.0048 28  LYS   A CA  
739  C  C   A LYS   A 28  ? 0.3151 0.3352 0.2112 -0.0768 0.0535  -0.0370 28  LYS   A C   
740  C  C   B LYS   A 28  ? 0.2783 0.2978 0.2313 -0.0031 0.0181  -0.0006 28  LYS   A C   
741  O  O   A LYS   A 28  ? 0.3258 0.3407 0.2382 -0.0763 0.0362  -0.0366 28  LYS   A O   
742  O  O   B LYS   A 28  ? 0.2826 0.2993 0.2271 -0.0018 0.0105  0.0037  28  LYS   A O   
743  C  CB  A LYS   A 28  ? 0.3058 0.3192 0.2525 -0.0500 0.0350  -0.0663 28  LYS   A CB  
744  C  CB  B LYS   A 28  ? 0.2607 0.2824 0.2470 0.0133  0.0202  -0.0166 28  LYS   A CB  
745  C  CG  A LYS   A 28  ? 0.3221 0.3282 0.2915 -0.0377 0.0370  -0.0703 28  LYS   A CG  
746  C  CG  B LYS   A 28  ? 0.2661 0.2876 0.2683 0.0163  0.0228  -0.0199 28  LYS   A CG  
747  C  CD  A LYS   A 28  ? 0.3382 0.3439 0.3489 -0.0275 0.0370  -0.0613 28  LYS   A CD  
748  C  CD  B LYS   A 28  ? 0.2721 0.2948 0.2856 0.0179  0.0238  -0.0207 28  LYS   A CD  
749  C  CE  A LYS   A 28  ? 0.3521 0.3550 0.3907 -0.0222 0.0380  -0.0606 28  LYS   A CE  
750  C  CE  B LYS   A 28  ? 0.2787 0.3014 0.2981 0.0171  0.0248  -0.0231 28  LYS   A CE  
751  N  NZ  A LYS   A 28  ? 0.3613 0.3610 0.4161 -0.0175 0.0418  -0.0680 28  LYS   A NZ  
752  N  NZ  B LYS   A 28  ? 0.2834 0.3048 0.2980 0.0170  0.0262  -0.0280 28  LYS   A NZ  
779  N  N   A LYS   A 29  ? 0.3242 0.3584 0.2110 -0.0857 0.0909  -0.0172 29  LYS   A N   
780  N  N   B LYS   A 29  ? 0.2946 0.3155 0.2499 -0.0146 0.0270  0.0045  29  LYS   A N   
781  C  CA  A LYS   A 29  ? 0.3396 0.3854 0.2285 -0.0906 0.1153  -0.0053 29  LYS   A CA  
782  C  CA  B LYS   A 29  ? 0.3137 0.3344 0.2752 -0.0246 0.0327  0.0058  29  LYS   A CA  
783  C  C   A LYS   A 29  ? 0.3471 0.3871 0.2128 -0.0983 0.1016  0.0050  29  LYS   A C   
784  C  C   B LYS   A 29  ? 0.3211 0.3379 0.2617 -0.0350 0.0268  0.0148  29  LYS   A C   
785  O  O   A LYS   A 29  ? 0.3629 0.4012 0.2165 -0.0890 0.0990  0.0065  29  LYS   A O   
786  O  O   B LYS   A 29  ? 0.3286 0.3459 0.2696 -0.0340 0.0272  0.0165  29  LYS   A O   
787  C  CB  A LYS   A 29  ? 0.3502 0.4122 0.2834 -0.0807 0.1312  -0.0038 29  LYS   A CB  
788  C  CB  B LYS   A 29  ? 0.3229 0.3479 0.3128 -0.0230 0.0435  0.0023  29  LYS   A CB  
789  C  CG  A LYS   A 29  ? 0.3658 0.4363 0.3450 -0.0694 0.1345  0.0003  29  LYS   A CG  
790  C  CG  B LYS   A 29  ? 0.3326 0.3600 0.3505 -0.0207 0.0495  -0.0002 29  LYS   A CG  
791  C  CD  A LYS   A 29  ? 0.3795 0.4564 0.3992 -0.0604 0.1362  0.0016  29  LYS   A CD  
792  C  CD  B LYS   A 29  ? 0.3405 0.3712 0.3823 -0.0177 0.0516  -0.0031 29  LYS   A CD  
793  C  CE  A LYS   A 29  ? 0.3890 0.4708 0.4374 -0.0532 0.1364  -0.0007 29  LYS   A CE  
794  C  CE  B LYS   A 29  ? 0.3466 0.3805 0.4072 -0.0141 0.0535  -0.0086 29  LYS   A CE  
795  N  NZ  A LYS   A 29  ? 0.3933 0.4790 0.4648 -0.0485 0.1321  -0.0031 29  LYS   A NZ  
796  N  NZ  B LYS   A 29  ? 0.3500 0.3857 0.4195 -0.0114 0.0537  -0.0115 29  LYS   A NZ  
823  N  N   A VAL   A 30  ? 0.3366 0.3707 0.1867 -0.1131 0.0911  0.0103  30  VAL   A N   
824  N  N   B VAL   A 30  ? 0.3217 0.3329 0.2474 -0.0445 0.0217  0.0167  30  VAL   A N   
825  C  CA  A VAL   A 30  ? 0.3315 0.3517 0.1820 -0.1282 0.0599  0.0270  30  VAL   A CA  
826  C  CA  B VAL   A 30  ? 0.3232 0.3260 0.2385 -0.0535 0.0099  0.0228  30  VAL   A CA  
827  C  C   A VAL   A 30  ? 0.3310 0.3379 0.1503 -0.1253 0.0424  0.0378  30  VAL   A C   
828  C  C   B VAL   A 30  ? 0.3257 0.3223 0.2228 -0.0576 0.0021  0.0234  30  VAL   A C   
829  O  O   A VAL   A 30  ? 0.3418 0.3405 0.1554 -0.1207 0.0350  0.0425  30  VAL   A O   
830  O  O   B VAL   A 30  ? 0.3295 0.3230 0.2192 -0.0564 -0.0009 0.0250  30  VAL   A O   
831  C  CB  A VAL   A 30  ? 0.3276 0.3454 0.2143 -0.1448 0.0408  0.0272  30  VAL   A CB  
832  C  CB  B VAL   A 30  ? 0.3217 0.3216 0.2461 -0.0573 0.0034  0.0252  30  VAL   A CB  
833  C  CG1 A VAL   A 30  ? 0.3312 0.3427 0.2264 -0.1473 0.0312  0.0312  30  VAL   A CG1 
834  C  CG1 B VAL   A 30  ? 0.3227 0.3207 0.2511 -0.0575 0.0007  0.0269  30  VAL   A CG1 
835  C  CG2 A VAL   A 30  ? 0.3236 0.3452 0.2335 -0.1570 0.0401  0.0286  30  VAL   A CG2 
836  C  CG2 B VAL   A 30  ? 0.3210 0.3202 0.2521 -0.0601 0.0016  0.0276  30  VAL   A CG2 
855  N  N   A LYS   A 31  ? 0.3213 0.3222 0.1380 -0.1244 0.0162  0.0318  31  LYS   A N   
856  N  N   B LYS   A 31  ? 0.3245 0.3173 0.2201 -0.0631 -0.0073 0.0215  31  LYS   A N   
857  C  CA  A LYS   A 31  ? 0.3297 0.3203 0.1660 -0.1066 -0.0091 0.0298  31  LYS   A CA  
858  C  CA  B LYS   A 31  ? 0.3269 0.3163 0.2293 -0.0652 -0.0161 0.0229  31  LYS   A CA  
859  C  C   A LYS   A 31  ? 0.3086 0.3038 0.1303 -0.0895 -0.0175 0.0647  31  LYS   A C   
860  C  C   B LYS   A 31  ? 0.3065 0.2996 0.1772 -0.0705 -0.0191 0.0438  31  LYS   A C   
861  O  O   A LYS   A 31  ? 0.3165 0.3183 0.1461 -0.0838 -0.0241 0.0747  31  LYS   A O   
862  O  O   B LYS   A 31  ? 0.3121 0.3053 0.1854 -0.0679 -0.0236 0.0505  31  LYS   A O   
863  C  CB  A LYS   A 31  ? 0.3655 0.3402 0.2690 -0.0989 -0.0262 0.0035  31  LYS   A CB  
864  C  CB  B LYS   A 31  ? 0.3495 0.3320 0.2991 -0.0602 -0.0226 0.0082  31  LYS   A CB  
865  C  CG  A LYS   A 31  ? 0.4048 0.3633 0.3844 -0.0819 -0.0413 -0.0150 31  LYS   A CG  
866  C  CG  B LYS   A 31  ? 0.3718 0.3484 0.3727 -0.0526 -0.0292 -0.0030 31  LYS   A CG  
867  C  CD  A LYS   A 31  ? 0.4361 0.3818 0.4683 -0.0673 -0.0543 -0.0306 31  LYS   A CD  
868  C  CD  B LYS   A 31  ? 0.3890 0.3624 0.4305 -0.0461 -0.0358 -0.0126 31  LYS   A CD  
869  C  CE  A LYS   A 31  ? 0.4559 0.3962 0.5189 -0.0557 -0.0640 -0.0408 31  LYS   A CE  
870  C  CE  B LYS   A 31  ? 0.4000 0.3730 0.4657 -0.0411 -0.0403 -0.0187 31  LYS   A CE  
871  N  NZ  A LYS   A 31  ? 0.4662 0.4025 0.5508 -0.0483 -0.0717 -0.0468 31  LYS   A NZ  
872  N  NZ  B LYS   A 31  ? 0.4061 0.3782 0.4895 -0.0377 -0.0434 -0.0226 31  LYS   A NZ  
899  N  N   . PRO   A 32  ? 0.2798 0.2769 0.1309 -0.0794 -0.0157 0.0452  32  PRO   A N   
900  C  CA  . PRO   A 32  ? 0.2609 0.2540 0.1517 -0.0705 -0.0184 0.0591  32  PRO   A CA  
901  C  C   . PRO   A 32  ? 0.2494 0.2512 0.1665 -0.0565 -0.0268 0.0658  32  PRO   A C   
902  O  O   . PRO   A 32  ? 0.2403 0.2446 0.1807 -0.0576 -0.0386 0.0632  32  PRO   A O   
903  C  CB  . PRO   A 32  ? 0.2499 0.2535 0.1632 -0.0688 -0.0207 0.0422  32  PRO   A CB  
904  C  CG  . PRO   A 32  ? 0.2501 0.2582 0.1159 -0.0644 -0.0305 0.0294  32  PRO   A CG  
905  C  CD  . PRO   A 32  ? 0.2590 0.2670 0.1075 -0.0716 -0.0281 0.0374  32  PRO   A CD  
913  N  N   . THR   A 33  ? 0.2550 0.2489 0.1539 -0.0495 -0.0310 0.0677  33  THR   A N   
914  C  CA  . THR   A 33  ? 0.2528 0.2512 0.1624 -0.0371 -0.0439 0.0691  33  THR   A CA  
915  C  C   . THR   A 33  ? 0.2217 0.2285 0.1535 -0.0402 -0.0384 0.0535  33  THR   A C   
916  O  O   . THR   A 33  ? 0.2140 0.2305 0.1772 -0.0453 -0.0451 0.0512  33  THR   A O   
917  C  CB  . THR   A 33  ? 0.2803 0.2769 0.1861 -0.0275 -0.0427 0.0906  33  THR   A CB  
918  O  OG1 . THR   A 33  ? 0.3038 0.2945 0.2115 -0.0155 -0.0336 0.1021  33  THR   A OG1 
919  C  CG2 . THR   A 33  ? 0.2846 0.2848 0.2074 -0.0231 -0.0476 0.0888  33  THR   A CG2 
927  N  N   . VAL   A 34  ? 0.1943 0.2067 0.1425 -0.0426 -0.0280 0.0455  34  VAL   A N   
928  C  CA  . VAL   A 34  ? 0.1750 0.1879 0.1352 -0.0369 -0.0199 0.0369  34  VAL   A CA  
929  C  C   . VAL   A 34  ? 0.1672 0.1792 0.1266 -0.0300 -0.0056 0.0337  34  VAL   A C   
930  O  O   . VAL   A 34  ? 0.1681 0.1805 0.1607 -0.0363 -0.0037 0.0425  34  VAL   A O   
931  C  CB  . VAL   A 34  ? 0.1799 0.1841 0.1584 -0.0312 -0.0099 0.0259  34  VAL   A CB  
932  C  CG1 . VAL   A 34  ? 0.1843 0.1833 0.1732 -0.0263 -0.0012 0.0180  34  VAL   A CG1 
933  C  CG2 . VAL   A 34  ? 0.1869 0.1966 0.1893 -0.0224 -0.0150 0.0233  34  VAL   A CG2 
943  N  N   . VAL   A 35  ? 0.1531 0.1636 0.1311 -0.0327 -0.0123 0.0289  35  VAL   A N   
944  C  CA  . VAL   A 35  ? 0.1488 0.1618 0.1279 -0.0225 -0.0072 0.0225  35  VAL   A CA  
945  C  C   . VAL   A 35  ? 0.1446 0.1447 0.1259 -0.0196 0.0033  0.0244  35  VAL   A C   
946  O  O   . VAL   A 35  ? 0.1376 0.1587 0.1471 -0.0298 0.0103  0.0214  35  VAL   A O   
947  C  CB  . VAL   A 35  ? 0.1511 0.1660 0.1405 -0.0144 0.0050  0.0099  35  VAL   A CB  
948  C  CG1 . VAL   A 35  ? 0.1600 0.1703 0.1602 -0.0085 -0.0017 0.0057  35  VAL   A CG1 
949  C  CG2 . VAL   A 35  ? 0.1496 0.1677 0.1683 -0.0126 0.0083  0.0050  35  VAL   A CG2 
959  N  N   . VAL   A 36  ? 0.1310 0.1415 0.1268 -0.0191 0.0012  0.0248  36  VAL   A N   
960  C  CA  . VAL   A 36  ? 0.1243 0.1331 0.1263 -0.0131 0.0010  0.0134  36  VAL   A CA  
961  C  C   . VAL   A 36  ? 0.1224 0.1359 0.1338 -0.0129 0.0024  0.0128  36  VAL   A C   
962  O  O   . VAL   A 36  ? 0.1249 0.1351 0.1601 -0.0090 0.0149  0.0195  36  VAL   A O   
963  C  CB  . VAL   A 36  ? 0.1272 0.1247 0.1375 -0.0104 -0.0022 0.0154  36  VAL   A CB  
964  C  CG1 . VAL   A 36  ? 0.1299 0.1251 0.1626 -0.0142 0.0012  0.0027  36  VAL   A CG1 
965  C  CG2 . VAL   A 36  ? 0.1363 0.1326 0.1535 -0.0080 -0.0043 0.0208  36  VAL   A CG2 
975  N  N   . ASN   A 37  ? 0.1144 0.1248 0.1368 -0.0096 0.0052  0.0191  37  ASN   A N   
976  C  CA  . ASN   A 37  ? 0.1196 0.1221 0.1261 -0.0045 0.0048  0.0225  37  ASN   A CA  
977  C  C   . ASN   A 37  ? 0.1142 0.1209 0.1279 -0.0049 0.0136  0.0248  37  ASN   A C   
978  O  O   . ASN   A 37  ? 0.1289 0.1333 0.1375 0.0044  0.0141  0.0149  37  ASN   A O   
979  C  CB  . ASN   A 37  ? 0.1210 0.1208 0.1353 -0.0031 -0.0019 0.0150  37  ASN   A CB  
980  C  CG  . ASN   A 37  ? 0.1199 0.1239 0.1407 -0.0033 0.0066  0.0148  37  ASN   A CG  
981  O  OD1 . ASN   A 37  ? 0.1173 0.1266 0.1709 -0.0035 0.0044  0.0193  37  ASN   A OD1 
982  N  ND2 . ASN   A 37  ? 0.1274 0.1258 0.1431 -0.0024 0.0010  0.0258  37  ASN   A ND2 
989  N  N   A ALA   A 38  ? 0.1138 0.1289 0.1326 -0.0025 0.0134  0.0153  38  ALA   A N   
990  N  N   B ALA   A 38  ? 0.1181 0.1284 0.1262 -0.0043 0.0079  0.0203  38  ALA   A N   
991  C  CA  A ALA   A 38  ? 0.1263 0.1352 0.1335 -0.0044 0.0077  0.0073  38  ALA   A CA  
992  C  CA  B ALA   A 38  ? 0.1260 0.1343 0.1292 -0.0061 0.0003  0.0171  38  ALA   A CA  
993  C  C   A ALA   A 38  ? 0.1245 0.1336 0.1341 0.0001  -0.0011 0.0028  38  ALA   A C   
994  C  C   B ALA   A 38  ? 0.1235 0.1312 0.1319 -0.0031 -0.0024 0.0138  38  ALA   A C   
995  O  O   A ALA   A 38  ? 0.1244 0.1278 0.1488 0.0029  -0.0052 0.0050  38  ALA   A O   
996  O  O   B ALA   A 38  ? 0.1205 0.1292 0.1384 -0.0059 -0.0054 0.0219  38  ALA   A O   
997  C  CB  A ALA   A 38  ? 0.1342 0.1599 0.1358 -0.0152 -0.0045 0.0025  38  ALA   A CB  
998  C  CB  B ALA   A 38  ? 0.1329 0.1485 0.1314 -0.0097 -0.0114 0.0116  38  ALA   A CB  
1009 N  N   . ALA   A 39  ? 0.1225 0.1273 0.1437 0.0001  0.0048  0.0151  39  ALA   A N   
1010 C  CA  . ALA   A 39  ? 0.1271 0.1323 0.1358 -0.0001 0.0045  0.0050  39  ALA   A CA  
1011 C  C   . ALA   A 39  ? 0.1259 0.1238 0.1391 0.0012  0.0021  0.0069  39  ALA   A C   
1012 O  O   . ALA   A 39  ? 0.1362 0.1302 0.1422 -0.0081 0.0040  0.0085  39  ALA   A O   
1013 C  CB  . ALA   A 39  ? 0.1301 0.1586 0.1518 -0.0053 0.0012  0.0053  39  ALA   A CB  
1020 N  N   A ASN   A 40  ? 0.1300 0.1341 0.1451 -0.0076 0.0147  0.0044  40  ASN   A N   
1021 N  N   B ASN   A 40  ? 0.1355 0.1218 0.1325 -0.0042 0.0173  0.0124  40  ASN   A N   
1022 C  CA  A ASN   A 40  ? 0.1293 0.1263 0.1467 -0.0006 0.0033  0.0016  40  ASN   A CA  
1023 C  CA  B ASN   A 40  ? 0.1449 0.1165 0.1322 -0.0035 0.0162  0.0159  40  ASN   A CA  
1024 C  C   A ASN   A 40  ? 0.1297 0.1200 0.1374 -0.0011 0.0164  0.0113  40  ASN   A C   
1025 C  C   B ASN   A 40  ? 0.1432 0.1136 0.1177 -0.0056 0.0212  0.0359  40  ASN   A C   
1026 O  O   A ASN   A 40  ? 0.1278 0.1252 0.1409 -0.0040 0.0149  0.0105  40  ASN   A O   
1027 O  O   B ASN   A 40  ? 0.1432 0.1151 0.1279 -0.0093 0.0155  0.0374  40  ASN   A O   
1028 C  CB  A ASN   A 40  ? 0.1436 0.1371 0.1519 0.0039  -0.0002 0.0103  40  ASN   A CB  
1029 C  CB  B ASN   A 40  ? 0.1540 0.1197 0.1502 -0.0054 0.0216  0.0081  40  ASN   A CB  
1030 C  CG  A ASN   A 40  ? 0.1533 0.1374 0.1627 0.0051  -0.0016 0.0076  40  ASN   A CG  
1031 C  CG  B ASN   A 40  ? 0.1586 0.1256 0.1740 -0.0068 0.0235  0.0041  40  ASN   A CG  
1032 O  OD1 A ASN   A 40  ? 0.1615 0.1342 0.1920 0.0062  -0.0047 0.0100  40  ASN   A OD1 
1033 O  OD1 B ASN   A 40  ? 0.1619 0.1301 0.1818 -0.0106 0.0221  0.0080  40  ASN   A OD1 
1034 N  ND2 A ASN   A 40  ? 0.1553 0.1499 0.1538 0.0115  0.0016  -0.0091 40  ASN   A ND2 
1035 N  ND2 B ASN   A 40  ? 0.1588 0.1350 0.1790 -0.0080 0.0373  -0.0029 40  ASN   A ND2 
1048 N  N   A VAL   A 41  ? 0.1355 0.1228 0.1419 -0.0009 0.0111  0.0182  41  VAL   A N   
1049 N  N   B VAL   A 41  ? 0.1452 0.1179 0.1120 0.0026  0.0160  0.0399  41  VAL   A N   
1050 C  CA  A VAL   A 41  ? 0.1378 0.1287 0.1596 0.0039  0.0118  0.0146  41  VAL   A CA  
1051 C  CA  B VAL   A 41  ? 0.1476 0.1242 0.1173 0.0044  0.0252  0.0338  41  VAL   A CA  
1052 C  C   A VAL   A 41  ? 0.1344 0.1277 0.1604 0.0035  0.0177  0.0137  41  VAL   A C   
1053 C  C   B VAL   A 41  ? 0.1486 0.1262 0.1196 -0.0021 0.0281  0.0284  41  VAL   A C   
1054 O  O   A VAL   A 41  ? 0.1396 0.1227 0.1711 0.0007  0.0049  0.0054  41  VAL   A O   
1055 O  O   B VAL   A 41  ? 0.1506 0.1190 0.1127 -0.0057 0.0191  0.0209  41  VAL   A O   
1056 C  CB  A VAL   A 41  ? 0.1400 0.1325 0.1580 0.0065  0.0191  0.0147  41  VAL   A CB  
1057 C  CB  B VAL   A 41  ? 0.1536 0.1323 0.1332 0.0078  0.0316  0.0349  41  VAL   A CB  
1058 C  CG1 A VAL   A 41  ? 0.1524 0.1378 0.1718 0.0093  0.0104  0.0056  41  VAL   A CG1 
1059 C  CG1 B VAL   A 41  ? 0.1657 0.1323 0.1376 0.0059  0.0439  0.0341  41  VAL   A CG1 
1060 C  CG2 A VAL   A 41  ? 0.1473 0.1446 0.1379 0.0006  0.0314  0.0165  41  VAL   A CG2 
1061 C  CG2 B VAL   A 41  ? 0.1522 0.1398 0.1429 0.0126  0.0177  0.0371  41  VAL   A CG2 
1080 N  N   A TYR   A 42  ? 0.1289 0.1228 0.1810 -0.0013 0.0236  0.0161  42  TYR   A N   
1081 N  N   B TYR   A 42  ? 0.1417 0.1288 0.1345 0.0012  0.0318  0.0270  42  TYR   A N   
1082 C  CA  A TYR   A 42  ? 0.1401 0.1178 0.1840 -0.0055 0.0299  0.0247  42  TYR   A CA  
1083 C  CA  B TYR   A 42  ? 0.1441 0.1326 0.1475 0.0043  0.0271  0.0239  42  TYR   A CA  
1084 C  C   A TYR   A 42  ? 0.1307 0.1161 0.1688 -0.0059 0.0206  0.0261  42  TYR   A C   
1085 C  C   B TYR   A 42  ? 0.1380 0.1299 0.1469 0.0010  0.0213  0.0248  42  TYR   A C   
1086 O  O   A TYR   A 42  ? 0.1290 0.1161 0.1925 -0.0145 0.0143  0.0043  42  TYR   A O   
1087 O  O   B TYR   A 42  ? 0.1360 0.1344 0.1548 -0.0028 0.0233  0.0241  42  TYR   A O   
1088 C  CB  A TYR   A 42  ? 0.1612 0.1253 0.1726 -0.0056 0.0380  0.0383  42  TYR   A CB  
1089 C  CB  B TYR   A 42  ? 0.1552 0.1394 0.1498 0.0071  0.0170  0.0249  42  TYR   A CB  
1090 C  CG  A TYR   A 42  ? 0.1755 0.1334 0.1671 -0.0012 0.0300  0.0432  42  TYR   A CG  
1091 C  CG  B TYR   A 42  ? 0.1650 0.1461 0.1519 0.0109  0.0044  0.0214  42  TYR   A CG  
1092 C  CD1 A TYR   A 42  ? 0.1829 0.1452 0.1803 -0.0134 0.0333  0.0293  42  TYR   A CD1 
1093 C  CD1 B TYR   A 42  ? 0.1687 0.1498 0.1549 0.0062  0.0035  0.0164  42  TYR   A CD1 
1094 C  CD2 A TYR   A 42  ? 0.1852 0.1544 0.1847 0.0039  0.0318  0.0316  42  TYR   A CD2 
1095 C  CD2 B TYR   A 42  ? 0.1727 0.1580 0.1660 0.0151  0.0041  0.0130  42  TYR   A CD2 
1096 C  CE1 A TYR   A 42  ? 0.1931 0.1573 0.1784 -0.0118 0.0345  0.0266  42  TYR   A CE1 
1097 C  CE1 B TYR   A 42  ? 0.1732 0.1556 0.1558 0.0078  0.0056  0.0147  42  TYR   A CE1 
1098 C  CE2 A TYR   A 42  ? 0.1939 0.1665 0.1969 -0.0067 0.0329  0.0289  42  TYR   A CE2 
1099 C  CE2 B TYR   A 42  ? 0.1783 0.1633 0.1670 0.0150  0.0063  0.0078  42  TYR   A CE2 
1100 C  CZ  A TYR   A 42  ? 0.2009 0.1678 0.1820 -0.0119 0.0403  0.0252  42  TYR   A CZ  
1101 C  CZ  B TYR   A 42  ? 0.1798 0.1644 0.1609 0.0104  0.0116  0.0055  42  TYR   A CZ  
1102 O  OH  A TYR   A 42  ? 0.2088 0.1810 0.2023 -0.0131 0.0352  0.0139  42  TYR   A OH  
1103 O  OH  B TYR   A 42  ? 0.1822 0.1747 0.1652 0.0037  0.0133  -0.0001 42  TYR   A OH  
1122 N  N   . LEU   A 43  ? 0.1312 0.1210 0.1580 -0.0032 0.0148  0.0092  43  LEU   A N   
1123 C  CA  . LEU   A 43  ? 0.1256 0.1216 0.1541 -0.0050 0.0104  0.0042  43  LEU   A CA  
1124 C  C   . LEU   A 43  ? 0.1235 0.1273 0.1535 -0.0046 0.0062  0.0024  43  LEU   A C   
1125 O  O   . LEU   A 43  ? 0.1430 0.1272 0.1718 0.0050  -0.0058 0.0068  43  LEU   A O   
1126 C  CB  . LEU   A 43  ? 0.1316 0.1221 0.1696 -0.0102 0.0046  0.0110  43  LEU   A CB  
1127 C  CG  . LEU   A 43  ? 0.1388 0.1202 0.1683 -0.0049 0.0038  0.0108  43  LEU   A CG  
1128 C  CD1 . LEU   A 43  ? 0.1508 0.1250 0.1911 -0.0038 -0.0063 0.0134  43  LEU   A CD1 
1129 C  CD2 . LEU   A 43  ? 0.1519 0.1232 0.1771 -0.0025 0.0112  0.0198  43  LEU   A CD2 
1142 N  N   A LYS   A 44  ? 0.1353 0.1225 0.1620 -0.0022 0.0095  0.0103  44  LYS   A N   
1143 N  N   B LYS   A 44  ? 0.1354 0.1300 0.1607 -0.0032 0.0069  0.0071  44  LYS   A N   
1144 C  CA  A LYS   A 44  ? 0.1483 0.1176 0.1614 -0.0043 0.0135  0.0150  44  LYS   A CA  
1145 C  CA  B LYS   A 44  ? 0.1464 0.1334 0.1688 -0.0039 0.0079  0.0091  44  LYS   A CA  
1146 C  C   A LYS   A 44  ? 0.1370 0.1260 0.1364 0.0034  -0.0027 0.0091  44  LYS   A C   
1147 C  C   B LYS   A 44  ? 0.1348 0.1317 0.1495 -0.0014 -0.0010 0.0085  44  LYS   A C   
1148 O  O   A LYS   A 44  ? 0.1461 0.1439 0.1500 0.0029  -0.0034 -0.0006 44  LYS   A O   
1149 O  O   B LYS   A 44  ? 0.1370 0.1372 0.1511 -0.0053 0.0012  0.0018  44  LYS   A O   
1150 C  CB  A LYS   A 44  ? 0.1763 0.1384 0.1931 -0.0025 0.0260  0.0269  44  LYS   A CB  
1151 C  CB  B LYS   A 44  ? 0.1687 0.1505 0.2027 -0.0025 0.0155  0.0110  44  LYS   A CB  
1152 C  CG  A LYS   A 44  ? 0.2093 0.1694 0.2495 -0.0068 0.0473  0.0409  44  LYS   A CG  
1153 C  CG  B LYS   A 44  ? 0.1901 0.1743 0.2509 -0.0021 0.0236  0.0168  44  LYS   A CG  
1154 C  CD  A LYS   A 44  ? 0.2446 0.2208 0.3486 -0.0047 0.0352  0.0341  44  LYS   A CD  
1155 C  CD  B LYS   A 44  ? 0.2104 0.2033 0.3064 -0.0050 0.0156  0.0180  44  LYS   A CD  
1156 C  CE  A LYS   A 44  ? 0.2625 0.2520 0.4083 -0.0017 0.0292  0.0343  44  LYS   A CE  
1157 C  CE  B LYS   A 44  ? 0.2238 0.2241 0.3413 -0.0082 0.0118  0.0215  44  LYS   A CE  
1158 N  NZ  A LYS   A 44  ? 0.2726 0.2744 0.4341 -0.0029 0.0246  0.0331  44  LYS   A NZ  
1159 N  NZ  B LYS   A 44  ? 0.2347 0.2399 0.3629 -0.0151 0.0111  0.0200  44  LYS   A NZ  
1186 N  N   . HIS   A 45  ? 0.1237 0.1247 0.1534 0.0012  -0.0069 0.0156  45  HIS   A N   
1187 C  CA  . HIS   A 45  ? 0.1201 0.1280 0.1528 0.0013  -0.0080 0.0099  45  HIS   A CA  
1188 C  C   . HIS   A 45  ? 0.1299 0.1406 0.1596 0.0039  0.0004  0.0101  45  HIS   A C   
1189 O  O   . HIS   A 45  ? 0.1511 0.1525 0.2004 0.0203  -0.0076 -0.0017 45  HIS   A O   
1190 C  CB  . HIS   A 45  ? 0.1277 0.1267 0.1544 -0.0004 -0.0071 0.0010  45  HIS   A CB  
1191 C  CG  . HIS   A 45  ? 0.1193 0.1233 0.1422 -0.0064 0.0059  0.0156  45  HIS   A CG  
1192 N  ND1 . HIS   A 45  ? 0.1138 0.1294 0.1573 -0.0051 0.0001  0.0174  45  HIS   A ND1 
1193 C  CD2 . HIS   A 45  ? 0.1238 0.1249 0.1428 -0.0071 -0.0046 0.0182  45  HIS   A CD2 
1194 C  CE1 . HIS   A 45  ? 0.1189 0.1373 0.1459 -0.0048 -0.0044 0.0185  45  HIS   A CE1 
1195 N  NE2 . HIS   A 45  ? 0.1226 0.1418 0.1405 -0.0030 -0.0041 0.0202  45  HIS   A NE2 
1204 N  N   A GLY   A 46  ? 0.1430 0.1438 0.1721 0.0060  -0.0106 0.0166  46  GLY   A N   
1205 N  N   B GLY   A 46  ? 0.1390 0.1424 0.1581 0.0129  -0.0147 0.0156  46  GLY   A N   
1206 C  CA  A GLY   A 46  ? 0.1456 0.1497 0.1884 0.0111  -0.0156 0.0202  46  GLY   A CA  
1207 C  CA  B GLY   A 46  ? 0.1451 0.1419 0.1601 0.0179  -0.0260 0.0210  46  GLY   A CA  
1208 C  C   A GLY   A 46  ? 0.1487 0.1438 0.1980 0.0168  -0.0214 0.0264  46  GLY   A C   
1209 C  C   B GLY   A 46  ? 0.1510 0.1362 0.1576 0.0216  -0.0325 0.0255  46  GLY   A C   
1210 O  O   A GLY   A 46  ? 0.1465 0.1503 0.2440 0.0081  -0.0311 0.0094  46  GLY   A O   
1211 O  O   B GLY   A 46  ? 0.1557 0.1348 0.1828 0.0190  -0.0366 0.0266  46  GLY   A O   
1218 N  N   A GLY   A 47  ? 0.1550 0.1451 0.1817 0.0183  -0.0224 0.0099  47  GLY   A N   
1219 N  N   B GLY   A 47  ? 0.1502 0.1354 0.1496 0.0240  -0.0305 0.0118  47  GLY   A N   
1220 C  CA  A GLY   A 47  ? 0.1532 0.1440 0.1744 0.0145  -0.0386 -0.0052 47  GLY   A CA  
1221 C  CA  B GLY   A 47  ? 0.1513 0.1397 0.1473 0.0224  -0.0392 -0.0020 47  GLY   A CA  
1222 C  C   A GLY   A 47  ? 0.1466 0.1343 0.1700 0.0156  -0.0427 -0.0101 47  GLY   A C   
1223 C  C   B GLY   A 47  ? 0.1480 0.1413 0.1382 0.0213  -0.0352 -0.0144 47  GLY   A C   
1224 O  O   A GLY   A 47  ? 0.1449 0.1302 0.1818 0.0167  -0.0369 -0.0018 47  GLY   A O   
1225 O  O   B GLY   A 47  ? 0.1485 0.1410 0.1413 0.0227  -0.0354 -0.0020 47  GLY   A O   
1232 N  N   A GLY   A 48  ? 0.1408 0.1380 0.1817 0.0063  -0.0511 -0.0096 48  GLY   A N   
1233 N  N   B GLY   A 48  ? 0.1460 0.1489 0.1474 0.0131  -0.0340 -0.0203 48  GLY   A N   
1234 C  CA  A GLY   A 48  ? 0.1456 0.1325 0.2037 0.0037  -0.0399 -0.0109 48  GLY   A CA  
1235 C  CA  B GLY   A 48  ? 0.1418 0.1467 0.1578 0.0109  -0.0205 -0.0160 48  GLY   A CA  
1236 C  C   A GLY   A 48  ? 0.1346 0.1313 0.1853 0.0001  -0.0176 -0.0049 48  GLY   A C   
1237 C  C   B GLY   A 48  ? 0.1337 0.1464 0.1546 0.0066  -0.0035 -0.0066 48  GLY   A C   
1238 O  O   A GLY   A 48  ? 0.1488 0.1271 0.1808 0.0036  -0.0128 0.0000  48  GLY   A O   
1239 O  O   B GLY   A 48  ? 0.1436 0.1488 0.1541 0.0029  0.0029  -0.0081 48  GLY   A O   
1246 N  N   A VAL   A 49  ? 0.1211 0.1287 0.1784 -0.0074 -0.0111 -0.0028 49  VAL   A N   
1247 N  N   B VAL   A 49  ? 0.1194 0.1417 0.1546 0.0039  -0.0033 -0.0001 49  VAL   A N   
1248 C  CA  A VAL   A 49  ? 0.1350 0.1263 0.1708 -0.0070 0.0124  -0.0044 49  VAL   A CA  
1249 C  CA  B VAL   A 49  ? 0.1078 0.1350 0.1511 0.0025  0.0043  0.0094  49  VAL   A CA  
1250 C  C   A VAL   A 49  ? 0.1339 0.1157 0.1488 -0.0020 0.0086  0.0070  49  VAL   A C   
1251 C  C   B VAL   A 49  ? 0.1046 0.1257 0.1361 0.0040  0.0081  0.0090  49  VAL   A C   
1252 O  O   A VAL   A 49  ? 0.1411 0.1218 0.1548 -0.0043 0.0148  0.0040  49  VAL   A O   
1253 O  O   B VAL   A 49  ? 0.1064 0.1212 0.1393 0.0049  0.0127  0.0083  49  VAL   A O   
1254 C  CB  A VAL   A 49  ? 0.1526 0.1299 0.1875 -0.0061 0.0222  -0.0103 49  VAL   A CB  
1255 C  CB  B VAL   A 49  ? 0.0994 0.1266 0.1478 0.0057  0.0100  0.0085  49  VAL   A CB  
1256 C  CG1 A VAL   A 49  ? 0.1550 0.1227 0.1972 0.0049  0.0221  -0.0107 49  VAL   A CG1 
1257 C  CG1 B VAL   A 49  ? 0.0957 0.1242 0.1461 0.0184  0.0096  0.0121  49  VAL   A CG1 
1258 C  CG2 A VAL   A 49  ? 0.1631 0.1419 0.2301 -0.0184 0.0229  -0.0089 49  VAL   A CG2 
1259 C  CG2 B VAL   A 49  ? 0.1024 0.1291 0.1451 -0.0007 0.0236  0.0061  49  VAL   A CG2 
1278 N  N   A ALA   A 50  ? 0.1273 0.1162 0.1400 -0.0065 -0.0132 0.0065  50  ALA   A N   
1279 N  N   B ALA   A 50  ? 0.1059 0.1262 0.1224 0.0055  0.0020  0.0072  50  ALA   A N   
1280 C  CA  A ALA   A 50  ? 0.1225 0.1157 0.1416 -0.0103 -0.0038 0.0150  50  ALA   A CA  
1281 C  CA  B ALA   A 50  ? 0.1101 0.1247 0.1166 0.0002  -0.0082 0.0040  50  ALA   A CA  
1282 C  C   A ALA   A 50  ? 0.1216 0.1182 0.1408 -0.0101 -0.0004 0.0123  50  ALA   A C   
1283 C  C   B ALA   A 50  ? 0.1193 0.1277 0.1140 -0.0000 -0.0047 -0.0026 50  ALA   A C   
1284 O  O   A ALA   A 50  ? 0.1162 0.1183 0.1614 -0.0065 -0.0027 0.0074  50  ALA   A O   
1285 O  O   B ALA   A 50  ? 0.1196 0.1306 0.1219 0.0026  -0.0024 -0.0054 50  ALA   A O   
1286 C  CB  A ALA   A 50  ? 0.1242 0.1201 0.1375 -0.0077 0.0015  0.0004  50  ALA   A CB  
1287 C  CB  B ALA   A 50  ? 0.1116 0.1221 0.1107 0.0016  -0.0090 -0.0064 50  ALA   A CB  
1298 N  N   A GLY   A 51  ? 0.1249 0.1156 0.1555 0.0005  -0.0050 0.0134  51  GLY   A N   
1299 N  N   B GLY   A 51  ? 0.1269 0.1276 0.1256 0.0026  -0.0081 -0.0064 51  GLY   A N   
1300 C  CA  A GLY   A 51  ? 0.1364 0.1119 0.1570 0.0052  -0.0169 0.0112  51  GLY   A CA  
1301 C  CA  B GLY   A 51  ? 0.1332 0.1269 0.1307 0.0019  -0.0139 -0.0090 51  GLY   A CA  
1302 C  C   A GLY   A 51  ? 0.1234 0.1199 0.1542 0.0097  -0.0080 -0.0001 51  GLY   A C   
1303 C  C   B GLY   A 51  ? 0.1286 0.1308 0.1393 0.0027  -0.0093 -0.0098 51  GLY   A C   
1304 O  O   A GLY   A 51  ? 0.1223 0.1341 0.1717 0.0027  -0.0076 -0.0062 51  GLY   A O   
1305 O  O   B GLY   A 51  ? 0.1322 0.1370 0.1432 -0.0016 -0.0125 -0.0129 51  GLY   A O   
1312 N  N   . ALA   A 52  ? 0.1205 0.1333 0.1539 0.0021  -0.0022 -0.0143 52  ALA   A N   
1313 C  CA  . ALA   A 52  ? 0.1208 0.1449 0.1639 -0.0023 0.0086  -0.0102 52  ALA   A CA  
1314 C  C   . ALA   A 52  ? 0.1206 0.1414 0.1425 -0.0109 0.0033  -0.0061 52  ALA   A C   
1315 O  O   . ALA   A 52  ? 0.1325 0.1508 0.1622 -0.0053 0.0054  -0.0107 52  ALA   A O   
1316 C  CB  . ALA   A 52  ? 0.1308 0.1792 0.1900 -0.0137 0.0067  -0.0051 52  ALA   A CB  
1323 N  N   . LEU   A 53  ? 0.1184 0.1374 0.1455 -0.0090 0.0020  -0.0048 53  LEU   A N   
1324 C  CA  . LEU   A 53  ? 0.1354 0.1430 0.1316 -0.0073 0.0037  0.0033  53  LEU   A CA  
1325 C  C   . LEU   A 53  ? 0.1325 0.1463 0.1146 0.0009  0.0022  0.0107  53  LEU   A C   
1326 O  O   . LEU   A 53  ? 0.1412 0.1575 0.1406 -0.0137 0.0022  0.0055  53  LEU   A O   
1327 C  CB  . LEU   A 53  ? 0.1445 0.1440 0.1368 -0.0104 0.0049  0.0061  53  LEU   A CB  
1328 C  CG  . LEU   A 53  ? 0.1600 0.1423 0.1478 -0.0179 -0.0035 0.0103  53  LEU   A CG  
1329 C  CD1 . LEU   A 53  ? 0.1727 0.1556 0.1563 -0.0125 0.0048  0.0105  53  LEU   A CD1 
1330 C  CD2 . LEU   A 53  ? 0.1895 0.1585 0.1544 -0.0278 0.0071  0.0120  53  LEU   A CD2 
1342 N  N   A ASN   A 54  ? 0.1236 0.1322 0.1304 -0.0045 -0.0063 0.0059  54  ASN   A N   
1343 N  N   B ASN   A 54  ? 0.1298 0.1441 0.1138 0.0074  -0.0030 0.0059  54  ASN   A N   
1344 C  CA  A ASN   A 54  ? 0.1125 0.1289 0.1465 -0.0062 -0.0050 0.0011  54  ASN   A CA  
1345 C  CA  B ASN   A 54  ? 0.1240 0.1452 0.1186 0.0117  -0.0029 0.0008  54  ASN   A CA  
1346 C  C   A ASN   A 54  ? 0.1245 0.1306 0.1400 -0.0142 0.0035  -0.0019 54  ASN   A C   
1347 C  C   B ASN   A 54  ? 0.1328 0.1456 0.1190 0.0066  -0.0001 -0.0044 54  ASN   A C   
1348 O  O   A ASN   A 54  ? 0.1235 0.1430 0.1552 -0.0156 -0.0026 -0.0076 54  ASN   A O   
1349 O  O   B ASN   A 54  ? 0.1325 0.1506 0.1205 0.0053  -0.0018 -0.0065 54  ASN   A O   
1350 C  CB  A ASN   A 54  ? 0.1128 0.1259 0.1568 -0.0125 -0.0093 -0.0017 54  ASN   A CB  
1351 C  CB  B ASN   A 54  ? 0.1178 0.1450 0.1131 0.0181  -0.0017 0.0002  54  ASN   A CB  
1352 C  CG  A ASN   A 54  ? 0.1169 0.1247 0.1662 -0.0080 -0.0037 0.0029  54  ASN   A CG  
1353 C  CG  B ASN   A 54  ? 0.1162 0.1422 0.1122 0.0218  0.0040  -0.0041 54  ASN   A CG  
1354 O  OD1 A ASN   A 54  ? 0.1182 0.1272 0.1501 -0.0139 -0.0119 0.0139  54  ASN   A OD1 
1355 O  OD1 B ASN   A 54  ? 0.1173 0.1494 0.1310 0.0170  -0.0029 -0.0092 54  ASN   A OD1 
1356 N  ND2 A ASN   A 54  ? 0.1170 0.1258 0.1861 -0.0073 -0.0059 0.0049  54  ASN   A ND2 
1357 N  ND2 B ASN   A 54  ? 0.1165 0.1348 0.1105 0.0189  0.0078  0.0018  54  ASN   A ND2 
1370 N  N   A LYS   A 55  ? 0.1282 0.1343 0.1522 -0.0107 -0.0036 -0.0092 55  LYS   A N   
1371 N  N   B LYS   A 55  ? 0.1376 0.1446 0.1281 0.0065  -0.0027 -0.0091 55  LYS   A N   
1372 C  CA  A LYS   A 55  ? 0.1333 0.1444 0.1605 -0.0003 -0.0081 -0.0197 55  LYS   A CA  
1373 C  CA  B LYS   A 55  ? 0.1443 0.1486 0.1438 0.0103  -0.0044 -0.0100 55  LYS   A CA  
1374 C  C   A LYS   A 55  ? 0.1293 0.1528 0.1625 -0.0040 0.0000  -0.0223 55  LYS   A C   
1375 C  C   B LYS   A 55  ? 0.1411 0.1545 0.1511 0.0008  -0.0021 -0.0160 55  LYS   A C   
1376 O  O   A LYS   A 55  ? 0.1321 0.1689 0.1773 -0.0003 -0.0026 -0.0240 55  LYS   A O   
1377 O  O   B LYS   A 55  ? 0.1455 0.1597 0.1507 0.0036  -0.0038 -0.0173 55  LYS   A O   
1378 C  CB  A LYS   A 55  ? 0.1372 0.1541 0.1765 0.0117  -0.0052 -0.0293 55  LYS   A CB  
1379 C  CB  B LYS   A 55  ? 0.1510 0.1524 0.1643 0.0154  -0.0026 -0.0007 55  LYS   A CB  
1380 C  CG  A LYS   A 55  ? 0.1539 0.1810 0.1824 0.0224  -0.0205 -0.0297 55  LYS   A CG  
1381 C  CG  B LYS   A 55  ? 0.1611 0.1634 0.1863 0.0223  -0.0085 -0.0025 55  LYS   A CG  
1382 C  CD  A LYS   A 55  ? 0.1699 0.2055 0.1859 0.0361  -0.0166 -0.0297 55  LYS   A CD  
1383 C  CD  B LYS   A 55  ? 0.1724 0.1741 0.2100 0.0272  -0.0040 -0.0060 55  LYS   A CD  
1384 C  CE  A LYS   A 55  ? 0.1932 0.2357 0.2028 0.0468  -0.0311 -0.0307 55  LYS   A CE  
1385 C  CE  B LYS   A 55  ? 0.1896 0.1898 0.2349 0.0285  -0.0062 -0.0117 55  LYS   A CE  
1386 N  NZ  A LYS   A 55  ? 0.2008 0.2483 0.2072 0.0551  -0.0445 -0.0308 55  LYS   A NZ  
1387 N  NZ  B LYS   A 55  ? 0.1966 0.1987 0.2438 0.0309  -0.0086 -0.0196 55  LYS   A NZ  
1414 N  N   . ALA   A 56  ? 0.1387 0.1617 0.1568 -0.0121 0.0014  -0.0174 56  ALA   A N   
1415 C  CA  . ALA   A 56  ? 0.1482 0.1809 0.1516 -0.0159 0.0093  -0.0148 56  ALA   A CA  
1416 C  C   . ALA   A 56  ? 0.1504 0.1935 0.1294 -0.0132 0.0163  -0.0208 56  ALA   A C   
1417 O  O   . ALA   A 56  ? 0.1584 0.2271 0.1467 -0.0008 0.0176  -0.0122 56  ALA   A O   
1418 C  CB  . ALA   A 56  ? 0.1553 0.1968 0.1655 -0.0174 0.0081  -0.0049 56  ALA   A CB  
1425 N  N   . THR   A 57  ? 0.1398 0.1746 0.1337 -0.0116 0.0057  -0.0159 57  THR   A N   
1426 C  CA  . THR   A 57  ? 0.1471 0.1687 0.1323 -0.0123 0.0010  -0.0110 57  THR   A CA  
1427 C  C   . THR   A 57  ? 0.1433 0.1751 0.1470 -0.0081 -0.0003 -0.0179 57  THR   A C   
1428 O  O   . THR   A 57  ? 0.1389 0.1780 0.1674 -0.0136 -0.0110 -0.0226 57  THR   A O   
1429 C  CB  . THR   A 57  ? 0.1424 0.1668 0.1387 -0.0138 -0.0014 -0.0119 57  THR   A CB  
1430 O  OG1 . THR   A 57  ? 0.1308 0.1600 0.1451 -0.0093 0.0021  -0.0075 57  THR   A OG1 
1431 C  CG2 . THR   A 57  ? 0.1473 0.1655 0.1343 -0.0107 -0.0017 0.0061  57  THR   A CG2 
1439 N  N   . ASN   A 58  ? 0.1438 0.1707 0.1710 -0.0113 0.0019  -0.0282 58  ASN   A N   
1440 C  CA  . ASN   A 58  ? 0.1643 0.1616 0.1902 -0.0150 0.0097  -0.0401 58  ASN   A CA  
1441 C  C   . ASN   A 58  ? 0.1399 0.1494 0.1772 -0.0036 -0.0050 -0.0238 58  ASN   A C   
1442 O  O   . ASN   A 58  ? 0.1434 0.1630 0.1897 -0.0126 -0.0082 -0.0306 58  ASN   A O   
1443 C  CB  . ASN   A 58  ? 0.2168 0.1779 0.2308 -0.0243 0.0332  -0.0529 58  ASN   A CB  
1444 C  CG  . ASN   A 58  ? 0.2624 0.2017 0.3079 -0.0194 0.0440  -0.0391 58  ASN   A CG  
1445 O  OD1 . ASN   A 58  ? 0.2914 0.1939 0.3518 0.0154  0.0811  -0.0211 58  ASN   A OD1 
1446 N  ND2 . ASN   A 58  ? 0.2731 0.2135 0.3342 -0.0203 0.0281  -0.0493 58  ASN   A ND2 
1453 N  N   . ASN   A 59  ? 0.1251 0.1413 0.1645 -0.0086 -0.0101 -0.0105 59  ASN   A N   
1454 C  CA  . ASN   A 59  ? 0.1307 0.1321 0.1704 -0.0050 -0.0067 -0.0083 59  ASN   A CA  
1455 C  C   . ASN   A 59  ? 0.1322 0.1359 0.1458 -0.0055 -0.0070 -0.0100 59  ASN   A C   
1456 O  O   . ASN   A 59  ? 0.1342 0.1390 0.1553 -0.0084 -0.0029 0.0015  59  ASN   A O   
1457 C  CB  . ASN   A 59  ? 0.1347 0.1316 0.1683 0.0013  -0.0178 -0.0146 59  ASN   A CB  
1458 C  CG  . ASN   A 59  ? 0.1363 0.1368 0.1712 -0.0045 -0.0243 0.0021  59  ASN   A CG  
1459 O  OD1 . ASN   A 59  ? 0.1512 0.1437 0.1649 -0.0135 -0.0248 0.0062  59  ASN   A OD1 
1460 N  ND2 . ASN   A 59  ? 0.1468 0.1398 0.1800 -0.0135 -0.0192 0.0036  59  ASN   A ND2 
1467 N  N   . ALA   A 60  ? 0.1256 0.1442 0.1557 -0.0029 -0.0033 -0.0049 60  ALA   A N   
1468 C  CA  . ALA   A 60  ? 0.1220 0.1465 0.1528 -0.0046 -0.0084 -0.0031 60  ALA   A CA  
1469 C  C   . ALA   A 60  ? 0.1257 0.1388 0.1588 -0.0081 -0.0088 0.0004  60  ALA   A C   
1470 O  O   . ALA   A 60  ? 0.1212 0.1370 0.1884 -0.0070 -0.0139 -0.0058 60  ALA   A O   
1471 C  CB  . ALA   A 60  ? 0.1353 0.1572 0.1561 -0.0016 -0.0108 -0.0214 60  ALA   A CB  
1477 N  N   . MET   A 61  ? 0.1235 0.1368 0.1544 -0.0096 -0.0022 -0.0011 61  MET   A N   
1478 C  CA  . MET   A 61  ? 0.1212 0.1313 0.1475 -0.0066 -0.0001 -0.0000 61  MET   A CA  
1479 C  C   . MET   A 61  ? 0.1190 0.1301 0.1548 -0.0074 -0.0055 -0.0064 61  MET   A C   
1480 O  O   . MET   A 61  ? 0.1246 0.1261 0.1701 -0.0060 0.0067  0.0074  61  MET   A O   
1481 C  CB  . MET   A 61  ? 0.1278 0.1331 0.1344 -0.0036 0.0041  -0.0009 61  MET   A CB  
1482 C  CG  . MET   A 61  ? 0.1276 0.1401 0.1568 -0.0016 0.0012  0.0043  61  MET   A CG  
1483 S  SD  . MET   A 61  ? 0.1314 0.1390 0.1943 -0.0110 -0.0037 -0.0132 61  MET   A SD  
1484 C  CE  . MET   A 61  ? 0.1540 0.1488 0.2121 -0.0117 0.0087  -0.0111 61  MET   A CE  
1494 N  N   . GLN   A 62  ? 0.1223 0.1235 0.1642 -0.0113 -0.0054 0.0028  62  GLN   A N   
1495 C  CA  . GLN   A 62  ? 0.1245 0.1184 0.1662 -0.0047 -0.0051 0.0052  62  GLN   A CA  
1496 C  C   . GLN   A 62  ? 0.1291 0.1106 0.1644 0.0010  0.0102  0.0027  62  GLN   A C   
1497 O  O   . GLN   A 62  ? 0.1279 0.1300 0.1533 -0.0043 0.0033  -0.0023 62  GLN   A O   
1498 C  CB  . GLN   A 62  ? 0.1249 0.1226 0.1615 -0.0014 -0.0010 0.0052  62  GLN   A CB  
1499 C  CG  . GLN   A 62  ? 0.1291 0.1236 0.1540 -0.0043 -0.0021 0.0113  62  GLN   A CG  
1500 C  CD  . GLN   A 62  ? 0.1323 0.1231 0.1583 -0.0002 0.0040  0.0086  62  GLN   A CD  
1501 O  OE1 . GLN   A 62  ? 0.1369 0.1395 0.1618 -0.0043 -0.0003 0.0077  62  GLN   A OE1 
1502 N  NE2 . GLN   A 62  ? 0.1393 0.1285 0.1770 0.0001  -0.0009 -0.0029 62  GLN   A NE2 
1511 N  N   . VAL   A 63  ? 0.1240 0.1212 0.1833 -0.0081 0.0108  -0.0167 63  VAL   A N   
1512 C  CA  . VAL   A 63  ? 0.1239 0.1327 0.2017 -0.0126 0.0013  -0.0079 63  VAL   A CA  
1513 C  C   . VAL   A 63  ? 0.1161 0.1339 0.1837 -0.0119 -0.0069 -0.0096 63  VAL   A C   
1514 O  O   . VAL   A 63  ? 0.1191 0.1350 0.2043 -0.0152 -0.0065 -0.0011 63  VAL   A O   
1515 C  CB  . VAL   A 63  ? 0.1363 0.1487 0.2293 -0.0130 -0.0032 -0.0344 63  VAL   A CB  
1516 C  CG1 . VAL   A 63  ? 0.1519 0.1700 0.2590 -0.0104 -0.0133 -0.0536 63  VAL   A CG1 
1517 C  CG2 . VAL   A 63  ? 0.1427 0.1464 0.2310 -0.0078 0.0041  -0.0298 63  VAL   A CG2 
1527 N  N   . GLU   A 64  ? 0.1233 0.1400 0.1681 -0.0024 -0.0065 -0.0029 64  GLU   A N   
1528 C  CA  . GLU   A 64  ? 0.1210 0.1389 0.1770 -0.0045 -0.0096 0.0073  64  GLU   A CA  
1529 C  C   . GLU   A 64  ? 0.1144 0.1340 0.1728 -0.0073 -0.0002 0.0122  64  GLU   A C   
1530 O  O   . GLU   A 64  ? 0.1223 0.1387 0.1828 -0.0056 -0.0020 0.0043  64  GLU   A O   
1531 C  CB  . GLU   A 64  ? 0.1273 0.1454 0.1840 -0.0076 -0.0027 0.0031  64  GLU   A CB  
1532 C  CG  . GLU   A 64  ? 0.1404 0.1527 0.1989 -0.0100 0.0043  0.0059  64  GLU   A CG  
1533 C  CD  . GLU   A 64  ? 0.1522 0.1592 0.1976 -0.0126 0.0073  0.0068  64  GLU   A CD  
1534 O  OE1 . GLU   A 64  ? 0.1511 0.1698 0.2184 -0.0177 0.0119  0.0094  64  GLU   A OE1 
1535 O  OE2 . GLU   A 64  ? 0.1688 0.1618 0.1831 -0.0251 -0.0079 0.0089  64  GLU   A OE2 
1542 N  N   . SER   A 65  ? 0.1107 0.1326 0.1627 0.0009  -0.0032 0.0056  65  SER   A N   
1543 C  CA  . SER   A 65  ? 0.1217 0.1268 0.1587 -0.0037 -0.0028 0.0013  65  SER   A CA  
1544 C  C   . SER   A 65  ? 0.1231 0.1371 0.1537 -0.0048 -0.0003 0.0040  65  SER   A C   
1545 O  O   . SER   A 65  ? 0.1319 0.1434 0.1790 0.0009  0.0150  -0.0051 65  SER   A O   
1546 C  CB  . SER   A 65  ? 0.1224 0.1259 0.1598 -0.0071 0.0006  0.0075  65  SER   A CB  
1547 O  OG  . SER   A 65  ? 0.1224 0.1372 0.1745 -0.0106 -0.0037 0.0159  65  SER   A OG  
1553 N  N   . ASP   A 66  ? 0.1229 0.1301 0.1704 -0.0041 0.0145  0.0127  66  ASP   A N   
1554 C  CA  . ASP   A 66  ? 0.1311 0.1423 0.1842 -0.0034 0.0104  0.0218  66  ASP   A CA  
1555 C  C   . ASP   A 66  ? 0.1287 0.1394 0.1941 -0.0060 0.0104  0.0204  66  ASP   A C   
1556 O  O   . ASP   A 66  ? 0.1334 0.1472 0.2088 -0.0073 0.0236  0.0239  66  ASP   A O   
1557 C  CB  . ASP   A 66  ? 0.1406 0.1503 0.2100 0.0052  0.0177  0.0306  66  ASP   A CB  
1558 C  CG  . ASP   A 66  ? 0.1622 0.1627 0.2389 -0.0063 0.0057  0.0550  66  ASP   A CG  
1559 O  OD1 . ASP   A 66  ? 0.1620 0.1905 0.2209 -0.0138 -0.0047 0.0518  66  ASP   A OD1 
1560 O  OD2 . ASP   A 66  ? 0.1840 0.1791 0.3208 0.0151  -0.0107 0.0326  66  ASP   A OD2 
1565 N  N   . ASP   A 67  ? 0.1258 0.1399 0.2027 -0.0006 0.0093  0.0234  67  ASP   A N   
1566 C  CA  . ASP   A 67  ? 0.1257 0.1554 0.2122 -0.0043 0.0043  0.0255  67  ASP   A CA  
1567 C  C   . ASP   A 67  ? 0.1231 0.1559 0.2062 0.0001  0.0043  0.0285  67  ASP   A C   
1568 O  O   . ASP   A 67  ? 0.1232 0.1595 0.2299 0.0027  0.0186  0.0330  67  ASP   A O   
1569 C  CB  . ASP   A 67  ? 0.1365 0.1665 0.2463 -0.0094 -0.0090 0.0323  67  ASP   A CB  
1570 C  CG  . ASP   A 67  ? 0.1292 0.1776 0.2884 -0.0112 -0.0234 0.0427  67  ASP   A CG  
1571 O  OD1 . ASP   A 67  ? 0.1387 0.1932 0.3594 -0.0139 -0.0375 0.0596  67  ASP   A OD1 
1572 O  OD2 . ASP   A 67  ? 0.1354 0.1822 0.2720 -0.0035 -0.0142 0.0269  67  ASP   A OD2 
1577 N  N   . TYR   A 68  ? 0.1267 0.1438 0.2087 0.0012  0.0129  0.0301  68  TYR   A N   
1578 C  CA  . TYR   A 68  ? 0.1394 0.1441 0.1960 0.0010  0.0160  0.0297  68  TYR   A CA  
1579 C  C   . TYR   A 68  ? 0.1330 0.1404 0.1925 -0.0026 0.0216  0.0194  68  TYR   A C   
1580 O  O   . TYR   A 68  ? 0.1380 0.1418 0.2121 0.0055  0.0279  0.0163  68  TYR   A O   
1581 C  CB  . TYR   A 68  ? 0.1420 0.1399 0.2146 0.0049  0.0334  0.0315  68  TYR   A CB  
1582 C  CG  . TYR   A 68  ? 0.1496 0.1562 0.2450 0.0005  0.0491  0.0335  68  TYR   A CG  
1583 C  CD1 . TYR   A 68  ? 0.1576 0.1627 0.2849 -0.0230 0.0379  -0.0090 68  TYR   A CD1 
1584 C  CD2 . TYR   A 68  ? 0.1727 0.1568 0.2918 0.0084  0.0547  0.0427  68  TYR   A CD2 
1585 C  CE1 . TYR   A 68  ? 0.1646 0.1675 0.3193 -0.0180 0.0474  -0.0154 68  TYR   A CE1 
1586 C  CE2 . TYR   A 68  ? 0.1679 0.1603 0.3094 -0.0019 0.0686  0.0129  68  TYR   A CE2 
1587 C  CZ  . TYR   A 68  ? 0.1660 0.1639 0.3283 -0.0192 0.0561  -0.0133 68  TYR   A CZ  
1588 O  OH  . TYR   A 68  ? 0.1912 0.1630 0.3493 -0.0151 0.0320  -0.0296 68  TYR   A OH  
1598 N  N   . ILE   A 69  ? 0.1267 0.1319 0.2004 -0.0037 0.0140  0.0221  69  ILE   A N   
1599 C  CA  . ILE   A 69  ? 0.1339 0.1382 0.1840 0.0015  0.0114  0.0124  69  ILE   A CA  
1600 C  C   . ILE   A 69  ? 0.1378 0.1397 0.1755 0.0048  0.0213  0.0169  69  ILE   A C   
1601 O  O   . ILE   A 69  ? 0.1433 0.1443 0.1857 -0.0003 0.0262  0.0171  69  ILE   A O   
1602 C  CB  . ILE   A 69  ? 0.1386 0.1566 0.1828 0.0033  0.0116  -0.0004 69  ILE   A CB  
1603 C  CG1 . ILE   A 69  ? 0.1391 0.1692 0.2011 0.0105  0.0124  -0.0107 69  ILE   A CG1 
1604 C  CG2 . ILE   A 69  ? 0.1623 0.1801 0.1947 0.0112  0.0030  -0.0178 69  ILE   A CG2 
1605 C  CD1 . ILE   A 69  ? 0.1405 0.1786 0.2246 -0.0082 0.0157  -0.0116 69  ILE   A CD1 
1617 N  N   . ALA   A 70  ? 0.1450 0.1388 0.1954 -0.0041 0.0201  0.0189  70  ALA   A N   
1618 C  CA  . ALA   A 70  ? 0.1459 0.1487 0.2114 -0.0142 0.0319  0.0273  70  ALA   A CA  
1619 C  C   . ALA   A 70  ? 0.1407 0.1666 0.2124 -0.0126 0.0313  0.0226  70  ALA   A C   
1620 O  O   . ALA   A 70  ? 0.1605 0.2050 0.2277 0.0101  0.0458  0.0413  70  ALA   A O   
1621 C  CB  . ALA   A 70  ? 0.1580 0.1459 0.2378 -0.0151 0.0255  0.0218  70  ALA   A CB  
1627 N  N   . THR   A 71  ? 0.1358 0.1639 0.2072 -0.0023 0.0228  0.0246  71  THR   A N   
1628 C  CA  . THR   A 71  ? 0.1448 0.1819 0.2327 0.0082  0.0185  0.0302  71  THR   A CA  
1629 C  C   . THR   A 71  ? 0.1346 0.1737 0.2551 0.0168  0.0309  0.0280  71  THR   A C   
1630 O  O   . THR   A 71  ? 0.1376 0.2000 0.3067 0.0088  0.0405  -0.0058 71  THR   A O   
1631 C  CB  . THR   A 71  ? 0.1730 0.2094 0.2671 0.0151  -0.0158 0.0401  71  THR   A CB  
1632 O  OG1 . THR   A 71  ? 0.1976 0.2282 0.2770 0.0082  -0.0333 0.0347  71  THR   A OG1 
1633 C  CG2 . THR   A 71  ? 0.1878 0.2297 0.2969 0.0226  -0.0294 0.0559  71  THR   A CG2 
1641 N  N   . ASN   A 72  ? 0.1405 0.1579 0.2262 0.0160  0.0236  0.0330  72  ASN   A N   
1642 C  CA  . ASN   A 72  ? 0.1452 0.1571 0.2281 0.0205  0.0340  0.0293  72  ASN   A CA  
1643 C  C   . ASN   A 72  ? 0.1562 0.1575 0.2264 0.0126  0.0506  0.0142  72  ASN   A C   
1644 O  O   . ASN   A 72  ? 0.1717 0.1605 0.2582 0.0163  0.0436  0.0010  72  ASN   A O   
1645 C  CB  . ASN   A 72  ? 0.1657 0.1611 0.2308 0.0206  0.0378  0.0279  72  ASN   A CB  
1646 C  CG  . ASN   A 72  ? 0.1906 0.1730 0.2419 0.0237  0.0403  0.0291  72  ASN   A CG  
1647 O  OD1 . ASN   A 72  ? 0.2076 0.2064 0.2575 0.0242  0.0432  0.0279  72  ASN   A OD1 
1648 N  ND2 . ASN   A 72  ? 0.2094 0.1706 0.2529 0.0501  0.0231  0.0236  72  ASN   A ND2 
1655 N  N   . GLY   A 73  ? 0.1563 0.1534 0.2205 0.0034  0.0439  0.0084  73  GLY   A N   
1656 C  CA  . GLY   A 73  ? 0.1620 0.1510 0.2009 -0.0058 0.0402  0.0100  73  GLY   A CA  
1657 C  C   . GLY   A 73  ? 0.1639 0.1423 0.1846 0.0011  0.0494  0.0255  73  GLY   A C   
1658 O  O   . GLY   A 73  ? 0.1659 0.1470 0.2051 0.0103  0.0339  0.0278  73  GLY   A O   
1662 N  N   . PRO   A 74  ? 0.1718 0.1458 0.1991 -0.0119 0.0507  0.0173  74  PRO   A N   
1663 C  CA  . PRO   A 74  ? 0.1691 0.1433 0.2085 -0.0044 0.0498  0.0166  74  PRO   A CA  
1664 C  C   . PRO   A 74  ? 0.1624 0.1285 0.1920 -0.0020 0.0377  0.0076  74  PRO   A C   
1665 O  O   . PRO   A 74  ? 0.1693 0.1329 0.2177 0.0038  0.0392  -0.0044 74  PRO   A O   
1666 C  CB  . PRO   A 74  ? 0.1842 0.1702 0.2382 0.0010  0.0463  0.0277  74  PRO   A CB  
1667 C  CG  . PRO   A 74  ? 0.2105 0.2069 0.2798 -0.0186 0.0331  0.0171  74  PRO   A CG  
1668 C  CD  . PRO   A 74  ? 0.1876 0.1791 0.2238 -0.0224 0.0364  0.0080  74  PRO   A CD  
1676 N  N   . LEU   A 75  ? 0.1607 0.1219 0.1757 -0.0030 0.0263  0.0048  75  LEU   A N   
1677 C  CA  . LEU   A 75  ? 0.1611 0.1240 0.1588 0.0025  0.0132  0.0114  75  LEU   A CA  
1678 C  C   . LEU   A 75  ? 0.1709 0.1383 0.1577 0.0050  0.0181  0.0139  75  LEU   A C   
1679 O  O   . LEU   A 75  ? 0.1995 0.1514 0.1627 0.0104  0.0101  0.0030  75  LEU   A O   
1680 C  CB  . LEU   A 75  ? 0.1640 0.1312 0.1542 -0.0097 0.0148  0.0194  75  LEU   A CB  
1681 C  CG  . LEU   A 75  ? 0.1813 0.1656 0.1681 -0.0397 0.0066  0.0085  75  LEU   A CG  
1682 C  CD1 . LEU   A 75  ? 0.1899 0.2182 0.1809 -0.0452 0.0134  -0.0072 75  LEU   A CD1 
1683 C  CD2 . LEU   A 75  ? 0.2092 0.2056 0.2248 -0.0154 0.0073  0.0031  75  LEU   A CD2 
1695 N  N   . LYS   A 76  ? 0.1694 0.1329 0.1769 -0.0071 0.0154  -0.0024 76  LYS   A N   
1696 C  CA  . LYS   A 76  ? 0.1640 0.1531 0.1876 -0.0105 0.0146  -0.0092 76  LYS   A CA  
1697 C  C   . LYS   A 76  ? 0.1621 0.1369 0.1509 -0.0038 0.0076  0.0075  76  LYS   A C   
1698 O  O   . LYS   A 76  ? 0.1637 0.1354 0.1614 0.0014  0.0110  0.0150  76  LYS   A O   
1699 C  CB  . LYS   A 76  ? 0.1671 0.1761 0.2201 0.0033  0.0153  -0.0352 76  LYS   A CB  
1700 C  CG  . LYS   A 76  ? 0.1784 0.1720 0.2698 0.0105  0.0084  -0.0266 76  LYS   A CG  
1701 C  CD  . LYS   A 76  ? 0.1864 0.1720 0.3148 0.0085  -0.0032 -0.0305 76  LYS   A CD  
1702 C  CE  . LYS   A 76  ? 0.2079 0.1900 0.3683 0.0016  0.0061  -0.0375 76  LYS   A CE  
1703 N  NZ  . LYS   A 76  ? 0.2092 0.1797 0.4080 -0.0173 0.0058  -0.0488 76  LYS   A NZ  
1717 N  N   . VAL   A 77  ? 0.1737 0.1440 0.1536 -0.0027 0.0232  0.0168  77  VAL   A N   
1718 C  CA  . VAL   A 77  ? 0.1665 0.1459 0.1520 0.0053  0.0138  0.0140  77  VAL   A CA  
1719 C  C   . VAL   A 77  ? 0.1595 0.1419 0.1546 0.0056  0.0076  0.0089  77  VAL   A C   
1720 O  O   . VAL   A 77  ? 0.1667 0.1473 0.1574 0.0095  0.0297  -0.0022 77  VAL   A O   
1721 C  CB  . VAL   A 77  ? 0.1827 0.1644 0.1538 0.0030  0.0104  0.0154  77  VAL   A CB  
1722 C  CG1 . VAL   A 77  ? 0.1799 0.1858 0.1675 0.0088  0.0022  0.0031  77  VAL   A CG1 
1723 C  CG2 . VAL   A 77  ? 0.2102 0.1762 0.1695 -0.0023 0.0013  0.0237  77  VAL   A CG2 
1733 N  N   . GLY   A 78  ? 0.1536 0.1348 0.1570 0.0030  0.0196  0.0094  78  GLY   A N   
1734 C  CA  . GLY   A 78  ? 0.1592 0.1298 0.1648 -0.0017 0.0225  0.0119  78  GLY   A CA  
1735 C  C   . GLY   A 78  ? 0.1451 0.1233 0.1643 0.0052  0.0184  0.0186  78  GLY   A C   
1736 O  O   . GLY   A 78  ? 0.1387 0.1343 0.1884 -0.0023 0.0164  0.0240  78  GLY   A O   
1740 N  N   . GLY   A 79  ? 0.1503 0.1222 0.1605 -0.0015 0.0155  0.0130  79  GLY   A N   
1741 C  CA  . GLY   A 79  ? 0.1482 0.1307 0.1726 0.0017  0.0148  0.0146  79  GLY   A CA  
1742 C  C   . GLY   A 79  ? 0.1337 0.1286 0.1596 -0.0019 0.0099  0.0106  79  GLY   A C   
1743 O  O   . GLY   A 79  ? 0.1338 0.1361 0.1765 0.0102  0.0141  0.0121  79  GLY   A O   
1747 N  N   . SER   A 80  ? 0.1294 0.1394 0.1777 -0.0002 0.0105  0.0009  80  SER   A N   
1748 C  CA  . SER   A 80  ? 0.1287 0.1347 0.1681 -0.0023 0.0047  0.0085  80  SER   A CA  
1749 C  C   . SER   A 80  ? 0.1243 0.1353 0.1668 -0.0060 0.0070  0.0146  80  SER   A C   
1750 O  O   . SER   A 80  ? 0.1259 0.1592 0.2073 0.0058  0.0107  0.0020  80  SER   A O   
1751 C  CB  . SER   A 80  ? 0.1418 0.1346 0.1921 -0.0070 0.0092  0.0105  80  SER   A CB  
1752 O  OG  . SER   A 80  ? 0.1685 0.1346 0.2303 0.0011  -0.0028 0.0247  80  SER   A OG  
1758 N  N   . CYS   A 81  ? 0.1213 0.1295 0.1673 -0.0030 -0.0034 0.0147  81  CYS   A N   
1759 C  CA  . CYS   A 81  ? 0.1234 0.1411 0.1641 -0.0082 -0.0026 0.0182  81  CYS   A CA  
1760 C  C   . CYS   A 81  ? 0.1220 0.1360 0.1654 -0.0099 -0.0013 0.0284  81  CYS   A C   
1761 O  O   . CYS   A 81  ? 0.1188 0.1673 0.1848 -0.0000 -0.0022 0.0399  81  CYS   A O   
1762 C  CB  . CYS   A 81  ? 0.1272 0.1418 0.1843 -0.0104 -0.0026 0.0234  81  CYS   A CB  
1763 S  SG  . CYS   A 81  ? 0.1436 0.1360 0.1801 -0.0149 0.0011  0.0164  81  CYS   A SG  
1769 N  N   . VAL   A 82  ? 0.1252 0.1399 0.1741 0.0003  -0.0158 0.0285  82  VAL   A N   
1770 C  CA  . VAL   A 82  ? 0.1379 0.1499 0.1675 0.0005  -0.0135 0.0327  82  VAL   A CA  
1771 C  C   . VAL   A 82  ? 0.1362 0.1549 0.1717 -0.0004 -0.0153 0.0295  82  VAL   A C   
1772 O  O   . VAL   A 82  ? 0.1298 0.1632 0.1978 0.0000  -0.0059 0.0036  82  VAL   A O   
1773 C  CB  . VAL   A 82  ? 0.1722 0.1597 0.1840 0.0023  -0.0077 0.0433  82  VAL   A CB  
1774 C  CG1 . VAL   A 82  ? 0.1896 0.1714 0.2035 0.0060  -0.0012 0.0313  82  VAL   A CG1 
1775 C  CG2 . VAL   A 82  ? 0.1779 0.1616 0.2164 -0.0025 -0.0053 0.0421  82  VAL   A CG2 
1785 N  N   . LEU   A 83  ? 0.1292 0.1520 0.1641 -0.0132 -0.0137 0.0197  83  LEU   A N   
1786 C  CA  . LEU   A 83  ? 0.1329 0.1482 0.1538 -0.0142 -0.0118 0.0143  83  LEU   A CA  
1787 C  C   . LEU   A 83  ? 0.1406 0.1531 0.1547 -0.0128 -0.0153 0.0194  83  LEU   A C   
1788 O  O   . LEU   A 83  ? 0.1483 0.1545 0.1666 -0.0181 -0.0128 0.0236  83  LEU   A O   
1789 C  CB  . LEU   A 83  ? 0.1399 0.1502 0.1636 -0.0151 -0.0145 0.0165  83  LEU   A CB  
1790 C  CG  . LEU   A 83  ? 0.1478 0.1625 0.1745 -0.0142 -0.0033 0.0102  83  LEU   A CG  
1791 C  CD1 . LEU   A 83  ? 0.1552 0.1664 0.1785 -0.0290 -0.0021 0.0226  83  LEU   A CD1 
1792 C  CD2 . LEU   A 83  ? 0.1453 0.1753 0.1775 -0.0151 0.0100  0.0163  83  LEU   A CD2 
1804 N  N   . SER   A 84  ? 0.1525 0.1579 0.1552 -0.0168 -0.0173 0.0260  84  SER   A N   
1805 C  CA  . SER   A 84  ? 0.1656 0.1652 0.1432 -0.0149 -0.0149 0.0241  84  SER   A CA  
1806 C  C   . SER   A 84  ? 0.1700 0.1672 0.1307 -0.0232 -0.0017 0.0131  84  SER   A C   
1807 O  O   . SER   A 84  ? 0.1637 0.1773 0.1345 -0.0168 -0.0086 0.0154  84  SER   A O   
1808 C  CB  . SER   A 84  ? 0.1692 0.1860 0.1494 -0.0157 -0.0156 0.0133  84  SER   A CB  
1809 O  OG  . SER   A 84  ? 0.1712 0.2084 0.1602 -0.0158 -0.0215 0.0027  84  SER   A OG  
1815 N  N   . GLY   A 85  ? 0.1818 0.1814 0.1418 -0.0240 0.0019  0.0152  85  GLY   A N   
1816 C  CA  . GLY   A 85  ? 0.1797 0.1869 0.1588 -0.0256 0.0154  0.0069  85  GLY   A CA  
1817 C  C   . GLY   A 85  ? 0.1721 0.1934 0.1444 -0.0231 0.0010  0.0048  85  GLY   A C   
1818 O  O   . GLY   A 85  ? 0.1767 0.1999 0.1519 -0.0307 0.0104  -0.0052 85  GLY   A O   
1822 N  N   . HIS   A 86  ? 0.1757 0.1852 0.1385 -0.0195 -0.0055 0.0062  86  HIS   A N   
1823 C  CA  . HIS   A 86  ? 0.1943 0.1927 0.1393 -0.0251 -0.0021 0.0062  86  HIS   A CA  
1824 C  C   . HIS   A 86  ? 0.2155 0.2067 0.1264 -0.0266 -0.0118 0.0082  86  HIS   A C   
1825 O  O   . HIS   A 86  ? 0.2302 0.2331 0.1332 -0.0247 0.0027  0.0079  86  HIS   A O   
1826 C  CB  . HIS   A 86  ? 0.1912 0.1805 0.1486 -0.0202 -0.0011 0.0060  86  HIS   A CB  
1827 C  CG  . HIS   A 86  ? 0.1846 0.1800 0.1440 -0.0099 -0.0002 0.0112  86  HIS   A CG  
1828 N  ND1 . HIS   A 86  ? 0.1941 0.1783 0.1820 -0.0176 -0.0031 0.0112  86  HIS   A ND1 
1829 C  CD2 . HIS   A 86  ? 0.1878 0.1762 0.1385 0.0021  0.0009  0.0182  86  HIS   A CD2 
1830 C  CE1 . HIS   A 86  ? 0.1912 0.1772 0.1787 -0.0119 0.0178  0.0130  86  HIS   A CE1 
1831 N  NE2 . HIS   A 86  ? 0.1889 0.1749 0.1628 0.0025  0.0164  0.0227  86  HIS   A NE2 
1839 N  N   . ASN   A 87  ? 0.2270 0.2126 0.1395 -0.0228 0.0079  -0.0058 87  ASN   A N   
1840 C  CA  . ASN   A 87  ? 0.2507 0.2244 0.1377 -0.0189 0.0301  -0.0089 87  ASN   A CA  
1841 C  C   . ASN   A 87  ? 0.2495 0.2403 0.1648 -0.0280 0.0512  0.0026  87  ASN   A C   
1842 O  O   . ASN   A 87  ? 0.2769 0.2583 0.2092 -0.0387 0.0837  -0.0063 87  ASN   A O   
1843 C  CB  . ASN   A 87  ? 0.2704 0.2366 0.1556 -0.0053 0.0310  -0.0083 87  ASN   A CB  
1844 C  CG  . ASN   A 87  ? 0.2827 0.2482 0.1666 0.0035  0.0482  -0.0043 87  ASN   A CG  
1845 O  OD1 . ASN   A 87  ? 0.2985 0.2441 0.1694 0.0174  0.0468  0.0067  87  ASN   A OD1 
1846 N  ND2 . ASN   A 87  ? 0.2870 0.2737 0.1713 0.0010  0.0520  -0.0000 87  ASN   A ND2 
1853 N  N   . LEU   A 88  ? 0.2174 0.2291 0.1655 -0.0318 0.0285  0.0055  88  LEU   A N   
1854 C  CA  . LEU   A 88  ? 0.1980 0.2285 0.1884 -0.0367 0.0286  0.0180  88  LEU   A CA  
1855 C  C   . LEU   A 88  ? 0.1915 0.2346 0.1750 -0.0346 0.0278  0.0283  88  LEU   A C   
1856 O  O   . LEU   A 88  ? 0.1959 0.2388 0.2035 -0.0328 0.0334  0.0473  88  LEU   A O   
1857 C  CB  . LEU   A 88  ? 0.1986 0.2337 0.1962 -0.0417 -0.0048 0.0259  88  LEU   A CB  
1858 C  CG  . LEU   A 88  ? 0.2199 0.2478 0.2254 -0.0432 -0.0109 0.0320  88  LEU   A CG  
1859 C  CD1 . LEU   A 88  ? 0.2316 0.2529 0.2223 -0.0444 -0.0112 0.0268  88  LEU   A CD1 
1860 C  CD2 . LEU   A 88  ? 0.2335 0.2595 0.2584 -0.0372 -0.0045 0.0242  88  LEU   A CD2 
1872 N  N   . ALA   A 89  ? 0.1915 0.2270 0.1541 -0.0306 0.0119  0.0079  89  ALA   A N   
1873 C  CA  . ALA   A 89  ? 0.1967 0.2240 0.1459 -0.0268 0.0057  0.0196  89  ALA   A CA  
1874 C  C   . ALA   A 89  ? 0.2037 0.2217 0.1472 -0.0213 -0.0113 0.0178  89  ALA   A C   
1875 O  O   . ALA   A 89  ? 0.2002 0.2158 0.1836 -0.0279 -0.0117 -0.0105 89  ALA   A O   
1876 C  CB  . ALA   A 89  ? 0.1877 0.2246 0.1385 -0.0285 0.0071  0.0188  89  ALA   A CB  
1882 N  N   . LYS   A 90  ? 0.2125 0.2389 0.1555 -0.0298 -0.0188 0.0212  90  LYS   A N   
1883 C  CA  . LYS   A 90  ? 0.2256 0.2582 0.1558 -0.0223 -0.0387 0.0268  90  LYS   A CA  
1884 C  C   . LYS   A 90  ? 0.2003 0.2376 0.1526 -0.0233 -0.0360 0.0174  90  LYS   A C   
1885 O  O   . LYS   A 90  ? 0.2024 0.2529 0.1877 -0.0252 -0.0401 0.0094  90  LYS   A O   
1886 C  CB  . LYS   A 90  ? 0.2596 0.3015 0.1907 -0.0201 -0.0550 0.0506  90  LYS   A CB  
1887 C  CG  . LYS   A 90  ? 0.3105 0.3453 0.2884 -0.0207 -0.0486 0.0608  90  LYS   A CG  
1888 C  CD  . LYS   A 90  ? 0.3751 0.3964 0.3926 -0.0241 -0.0280 0.0599  90  LYS   A CD  
1889 C  CE  . LYS   A 90  ? 0.4202 0.4363 0.4692 -0.0270 -0.0129 0.0574  90  LYS   A CE  
1890 N  NZ  . LYS   A 90  ? 0.4543 0.4598 0.5198 -0.0285 -0.0042 0.0588  90  LYS   A NZ  
1904 N  N   . HIS   A 91  ? 0.1873 0.2095 0.1251 -0.0207 -0.0395 0.0251  91  HIS   A N   
1905 C  CA  . HIS   A 91  ? 0.1729 0.1892 0.1353 -0.0134 -0.0293 0.0210  91  HIS   A CA  
1906 C  C   . HIS   A 91  ? 0.1565 0.1742 0.1216 -0.0149 -0.0149 0.0247  91  HIS   A C   
1907 O  O   . HIS   A 91  ? 0.1461 0.1875 0.1511 -0.0240 -0.0101 0.0268  91  HIS   A O   
1908 C  CB  . HIS   A 91  ? 0.1874 0.2151 0.1883 0.0077  -0.0425 0.0221  91  HIS   A CB  
1909 C  CG  . HIS   A 91  ? 0.2337 0.2674 0.2473 0.0173  -0.0701 0.0117  91  HIS   A CG  
1910 N  ND1 . HIS   A 91  ? 0.2482 0.2948 0.2901 0.0214  -0.0777 -0.0050 91  HIS   A ND1 
1911 C  CD2 . HIS   A 91  ? 0.2638 0.2906 0.2725 0.0238  -0.0838 0.0202  91  HIS   A CD2 
1912 C  CE1 . HIS   A 91  ? 0.2642 0.3072 0.3031 0.0254  -0.0759 0.0091  91  HIS   A CE1 
1913 N  NE2 . HIS   A 91  ? 0.2754 0.3059 0.2985 0.0301  -0.0845 0.0150  91  HIS   A NE2 
1921 N  N   . CYS   A 92  ? 0.1488 0.1646 0.1332 -0.0213 -0.0124 0.0246  92  CYS   A N   
1922 C  CA  . CYS   A 92  ? 0.1380 0.1575 0.1368 -0.0146 0.0002  0.0190  92  CYS   A CA  
1923 C  C   . CYS   A 92  ? 0.1327 0.1498 0.1357 -0.0164 -0.0005 0.0204  92  CYS   A C   
1924 O  O   . CYS   A 92  ? 0.1357 0.1511 0.1612 -0.0178 -0.0051 0.0168  92  CYS   A O   
1925 C  CB  . CYS   A 92  ? 0.1405 0.1559 0.1534 -0.0089 -0.0048 0.0115  92  CYS   A CB  
1926 S  SG  . CYS   A 92  ? 0.1395 0.1419 0.1415 -0.0129 -0.0058 0.0136  92  CYS   A SG  
1932 N  N   . LEU   A 93  ? 0.1332 0.1326 0.1462 -0.0104 0.0034  0.0198  93  LEU   A N   
1933 C  CA  . LEU   A 93  ? 0.1216 0.1338 0.1472 -0.0054 0.0000  0.0187  93  LEU   A CA  
1934 C  C   . LEU   A 93  ? 0.1251 0.1247 0.1368 0.0014  0.0038  0.0128  93  LEU   A C   
1935 O  O   . LEU   A 93  ? 0.1154 0.1321 0.1477 -0.0014 -0.0032 0.0115  93  LEU   A O   
1936 C  CB  . LEU   A 93  ? 0.1293 0.1352 0.1655 -0.0096 -0.0054 0.0273  93  LEU   A CB  
1937 C  CG  . LEU   A 93  ? 0.1363 0.1298 0.1690 -0.0049 -0.0024 0.0282  93  LEU   A CG  
1938 C  CD1 . LEU   A 93  ? 0.1391 0.1403 0.1964 0.0002  0.0089  0.0172  93  LEU   A CD1 
1939 C  CD2 . LEU   A 93  ? 0.1512 0.1306 0.1804 -0.0058 -0.0068 0.0129  93  LEU   A CD2 
1951 N  N   . HIS   A 94  ? 0.1143 0.1221 0.1424 -0.0027 0.0043  0.0210  94  HIS   A N   
1952 C  CA  . HIS   A 94  ? 0.1155 0.1194 0.1500 -0.0035 -0.0011 0.0201  94  HIS   A CA  
1953 C  C   . HIS   A 94  ? 0.1138 0.1186 0.1574 -0.0075 -0.0004 0.0140  94  HIS   A C   
1954 O  O   . HIS   A 94  ? 0.1152 0.1405 0.1863 -0.0029 0.0017  -0.0045 94  HIS   A O   
1955 C  CB  . HIS   A 94  ? 0.1128 0.1159 0.1570 -0.0046 -0.0049 0.0190  94  HIS   A CB  
1956 C  CG  . HIS   A 94  ? 0.1221 0.1185 0.1349 -0.0055 -0.0073 0.0175  94  HIS   A CG  
1957 N  ND1 . HIS   A 94  ? 0.1208 0.1201 0.1500 -0.0063 0.0007  0.0177  94  HIS   A ND1 
1958 C  CD2 . HIS   A 94  ? 0.1316 0.1332 0.1545 -0.0070 -0.0057 0.0084  94  HIS   A CD2 
1959 C  CE1 . HIS   A 94  ? 0.1256 0.1289 0.1493 -0.0105 -0.0077 0.0127  94  HIS   A CE1 
1960 N  NE2 . HIS   A 94  ? 0.1327 0.1283 0.1567 -0.0144 -0.0091 0.0027  94  HIS   A NE2 
1968 N  N   . VAL   A 95  ? 0.1122 0.1157 0.1330 -0.0035 0.0081  0.0085  95  VAL   A N   
1969 C  CA  . VAL   A 95  ? 0.1191 0.1172 0.1367 -0.0012 0.0078  0.0122  95  VAL   A CA  
1970 C  C   . VAL   A 95  ? 0.1216 0.1168 0.1241 -0.0123 -0.0007 0.0125  95  VAL   A C   
1971 O  O   . VAL   A 95  ? 0.1212 0.1273 0.1468 0.0065  -0.0000 0.0133  95  VAL   A O   
1972 C  CB  . VAL   A 95  ? 0.1200 0.1210 0.1526 -0.0077 0.0052  0.0077  95  VAL   A CB  
1973 C  CG1 . VAL   A 95  ? 0.1352 0.1281 0.1702 -0.0154 0.0002  0.0093  95  VAL   A CG1 
1974 C  CG2 . VAL   A 95  ? 0.1270 0.1281 0.1560 -0.0094 0.0097  0.0201  95  VAL   A CG2 
1984 N  N   . VAL   A 96  ? 0.1250 0.1170 0.1268 -0.0041 0.0017  0.0124  96  VAL   A N   
1985 C  CA  . VAL   A 96  ? 0.1349 0.1233 0.1383 -0.0003 0.0038  0.0158  96  VAL   A CA  
1986 C  C   . VAL   A 96  ? 0.1412 0.1297 0.1392 -0.0030 0.0140  0.0144  96  VAL   A C   
1987 O  O   . VAL   A 96  ? 0.1470 0.1347 0.1656 -0.0082 0.0153  0.0004  96  VAL   A O   
1988 C  CB  . VAL   A 96  ? 0.1360 0.1295 0.1420 -0.0014 0.0157  0.0126  96  VAL   A CB  
1989 C  CG1 . VAL   A 96  ? 0.1464 0.1351 0.1403 -0.0024 0.0142  0.0076  96  VAL   A CG1 
1990 C  CG2 . VAL   A 96  ? 0.1367 0.1370 0.1589 -0.0131 0.0176  0.0056  96  VAL   A CG2 
2000 N  N   . GLY   A 97  ? 0.1380 0.1311 0.1478 -0.0056 0.0099  0.0108  97  GLY   A N   
2001 C  CA  . GLY   A 97  ? 0.1463 0.1457 0.1352 -0.0077 -0.0011 0.0124  97  GLY   A CA  
2002 C  C   . GLY   A 97  ? 0.1437 0.1595 0.1363 -0.0141 0.0033  0.0091  97  GLY   A C   
2003 O  O   . GLY   A 97  ? 0.1628 0.1526 0.1536 -0.0107 -0.0004 0.0185  97  GLY   A O   
2007 N  N   . PRO   A 98  ? 0.1505 0.1629 0.1251 -0.0052 -0.0022 0.0203  98  PRO   A N   
2008 C  CA  . PRO   A 98  ? 0.1666 0.1929 0.1380 -0.0131 -0.0034 0.0059  98  PRO   A CA  
2009 C  C   . PRO   A 98  ? 0.1728 0.2006 0.1366 -0.0237 -0.0092 0.0333  98  PRO   A C   
2010 O  O   . PRO   A 98  ? 0.1622 0.1763 0.1679 -0.0181 -0.0073 0.0261  98  PRO   A O   
2011 C  CB  . PRO   A 98  ? 0.1801 0.2031 0.1234 -0.0053 -0.0060 -0.0026 98  PRO   A CB  
2012 C  CG  . PRO   A 98  ? 0.1775 0.1871 0.1411 -0.0025 -0.0015 -0.0078 98  PRO   A CG  
2013 C  CD  . PRO   A 98  ? 0.1605 0.1603 0.1314 0.0006  0.0019  0.0050  98  PRO   A CD  
2021 N  N   A ASN   A 99  ? 0.1761 0.2370 0.1388 -0.0289 -0.0102 0.0576  99  ASN   A N   
2022 N  N   B ASN   A 99  ? 0.1964 0.1970 0.1411 -0.0223 -0.0148 0.0478  99  ASN   A N   
2023 C  CA  A ASN   A 99  ? 0.1972 0.2585 0.1248 -0.0290 -0.0086 0.0765  99  ASN   A CA  
2024 C  CA  B ASN   A 99  ? 0.2249 0.1869 0.1409 -0.0179 -0.0179 0.0587  99  ASN   A CA  
2025 C  C   A ASN   A 99  ? 0.2167 0.2889 0.1282 -0.0402 -0.0105 0.0787  99  ASN   A C   
2026 C  C   B ASN   A 99  ? 0.2375 0.1812 0.1497 -0.0081 -0.0183 0.0526  99  ASN   A C   
2027 O  O   A ASN   A 99  ? 0.2246 0.3055 0.1404 -0.0255 -0.0113 0.0727  99  ASN   A O   
2028 O  O   B ASN   A 99  ? 0.2386 0.1601 0.1532 0.0060  -0.0219 0.0428  99  ASN   A O   
2029 C  CB  A ASN   A 99  ? 0.1927 0.2530 0.1462 -0.0279 -0.0180 0.0798  99  ASN   A CB  
2030 C  CB  B ASN   A 99  ? 0.2381 0.1862 0.1537 -0.0267 -0.0203 0.0700  99  ASN   A CB  
2031 C  CG  A ASN   A 99  ? 0.1909 0.2518 0.1529 -0.0206 -0.0243 0.0656  99  ASN   A CG  
2032 C  CG  B ASN   A 99  ? 0.2475 0.1868 0.1599 -0.0329 -0.0166 0.0822  99  ASN   A CG  
2033 O  OD1 A ASN   A 99  ? 0.2040 0.2600 0.1425 -0.0131 -0.0200 0.0553  99  ASN   A OD1 
2034 O  OD1 B ASN   A 99  ? 0.2527 0.1956 0.1489 -0.0309 -0.0130 0.0832  99  ASN   A OD1 
2035 N  ND2 A ASN   A 99  ? 0.1885 0.2400 0.1806 -0.0181 -0.0239 0.0790  99  ASN   A ND2 
2036 N  ND2 B ASN   A 99  ? 0.2513 0.1834 0.1914 -0.0333 -0.0222 0.0674  99  ASN   A ND2 
2049 N  N   A VAL   A 100 ? 0.2319 0.3026 0.1430 -0.0602 -0.0330 0.0667  100 VAL   A N   
2050 N  N   B VAL   A 100 ? 0.2496 0.2021 0.1634 -0.0088 -0.0224 0.0476  100 VAL   A N   
2051 C  CA  A VAL   A 100 ? 0.2530 0.3161 0.1585 -0.0676 -0.0437 0.0587  100 VAL   A CA  
2052 C  CA  B VAL   A 100 ? 0.2627 0.2200 0.1903 -0.0072 -0.0222 0.0372  100 VAL   A CA  
2053 C  C   A VAL   A 100 ? 0.2583 0.3263 0.1551 -0.0733 -0.0478 0.0782  100 VAL   A C   
2054 C  C   B VAL   A 100 ? 0.2620 0.2181 0.1914 0.0027  -0.0264 0.0299  100 VAL   A C   
2055 O  O   A VAL   A 100 ? 0.2640 0.3317 0.1750 -0.0689 -0.0321 0.0808  100 VAL   A O   
2056 O  O   B VAL   A 100 ? 0.2601 0.2088 0.1972 0.0033  -0.0277 0.0203  100 VAL   A O   
2057 C  CB  A VAL   A 100 ? 0.2720 0.3166 0.1867 -0.0695 -0.0463 0.0370  100 VAL   A CB  
2058 C  CB  B VAL   A 100 ? 0.2756 0.2360 0.2232 -0.0077 -0.0222 0.0282  100 VAL   A CB  
2059 C  CG1 A VAL   A 100 ? 0.2682 0.3183 0.2016 -0.0735 -0.0405 0.0318  100 VAL   A CG1 
2060 C  CG1 B VAL   A 100 ? 0.2774 0.2407 0.2377 -0.0070 -0.0248 0.0255  100 VAL   A CG1 
2061 C  CG2 A VAL   A 100 ? 0.2839 0.3166 0.1814 -0.0709 -0.0427 0.0211  100 VAL   A CG2 
2062 C  CG2 B VAL   A 100 ? 0.2805 0.2403 0.2389 -0.0087 -0.0169 0.0246  100 VAL   A CG2 
2081 N  N   A ASN   A 101 ? 0.2627 0.3360 0.1716 -0.0793 -0.0434 0.0993  101 ASN   A N   
2082 N  N   B ASN   A 101 ? 0.2681 0.2244 0.1937 0.0093  -0.0293 0.0286  101 ASN   A N   
2083 C  CA  A ASN   A 101 ? 0.2828 0.3449 0.1884 -0.0843 -0.0338 0.1223  101 ASN   A CA  
2084 C  CA  B ASN   A 101 ? 0.2769 0.2288 0.1945 0.0168  -0.0254 0.0287  101 ASN   A CA  
2085 C  C   A ASN   A 101 ? 0.3096 0.3766 0.2165 -0.0818 -0.0078 0.1433  101 ASN   A C   
2086 C  C   B ASN   A 101 ? 0.2911 0.2422 0.2027 0.0184  -0.0151 0.0421  101 ASN   A C   
2087 O  O   A ASN   A 101 ? 0.3267 0.3855 0.2566 -0.0779 -0.0094 0.1294  101 ASN   A O   
2088 O  O   B ASN   A 101 ? 0.2966 0.2421 0.1957 0.0171  -0.0159 0.0560  101 ASN   A O   
2089 C  CB  A ASN   A 101 ? 0.2788 0.3222 0.1832 -0.0875 -0.0533 0.1142  101 ASN   A CB  
2090 C  CB  B ASN   A 101 ? 0.2712 0.2226 0.1951 0.0181  -0.0237 0.0214  101 ASN   A CB  
2091 C  CG  A ASN   A 101 ? 0.2786 0.3058 0.1835 -0.0847 -0.0637 0.0800  101 ASN   A CG  
2092 C  CG  B ASN   A 101 ? 0.2702 0.2261 0.2143 0.0159  -0.0239 0.0160  101 ASN   A CG  
2093 O  OD1 A ASN   A 101 ? 0.2736 0.3043 0.1949 -0.0704 -0.0580 0.0458  101 ASN   A OD1 
2094 O  OD1 B ASN   A 101 ? 0.2748 0.2312 0.2323 0.0100  -0.0211 0.0150  101 ASN   A OD1 
2095 N  ND2 A ASN   A 101 ? 0.2852 0.2975 0.1815 -0.0946 -0.0613 0.0850  101 ASN   A ND2 
2096 N  ND2 B ASN   A 101 ? 0.2678 0.2251 0.2193 0.0207  -0.0218 0.0073  101 ASN   A ND2 
2109 N  N   A LYS   A 102 ? 0.3136 0.4033 0.2457 -0.0868 0.0121  0.1454  102 LYS   A N   
2110 N  N   B LYS   A 102 ? 0.2989 0.2561 0.2310 0.0189  0.0010  0.0405  102 LYS   A N   
2111 C  CA  A LYS   A 102 ? 0.3239 0.4264 0.2593 -0.0888 0.0162  0.1302  102 LYS   A CA  
2112 C  CA  B LYS   A 102 ? 0.3085 0.2698 0.2453 0.0151  0.0130  0.0379  102 LYS   A CA  
2113 C  C   A LYS   A 102 ? 0.3341 0.4468 0.2590 -0.0782 0.0150  0.1142  102 LYS   A C   
2114 C  C   B LYS   A 102 ? 0.3090 0.2701 0.2289 0.0165  0.0104  0.0548  102 LYS   A C   
2115 O  O   A LYS   A 102 ? 0.3370 0.4579 0.2685 -0.0754 0.0225  0.1052  102 LYS   A O   
2116 O  O   B LYS   A 102 ? 0.3091 0.2638 0.2205 0.0190  0.0129  0.0684  102 LYS   A O   
2117 C  CB  A LYS   A 102 ? 0.3304 0.4304 0.2924 -0.0973 0.0103  0.1142  102 LYS   A CB  
2118 C  CB  B LYS   A 102 ? 0.3177 0.2830 0.2872 0.0105  0.0169  0.0182  102 LYS   A CB  
2119 C  CG  A LYS   A 102 ? 0.3376 0.4329 0.3142 -0.1037 0.0024  0.1013  102 LYS   A CG  
2120 C  CG  B LYS   A 102 ? 0.3258 0.2945 0.3231 0.0069  0.0183  0.0022  102 LYS   A CG  
2121 C  CD  A LYS   A 102 ? 0.3486 0.4372 0.3397 -0.1048 -0.0017 0.0843  102 LYS   A CD  
2122 C  CD  B LYS   A 102 ? 0.3353 0.3069 0.3600 0.0034  0.0189  -0.0112 102 LYS   A CD  
2123 C  CE  A LYS   A 102 ? 0.3602 0.4407 0.3651 -0.1000 -0.0069 0.0742  102 LYS   A CE  
2124 C  CE  B LYS   A 102 ? 0.3432 0.3161 0.3860 0.0007  0.0186  -0.0202 102 LYS   A CE  
2125 N  NZ  A LYS   A 102 ? 0.3651 0.4408 0.3762 -0.1003 -0.0073 0.0682  102 LYS   A NZ  
2126 N  NZ  B LYS   A 102 ? 0.3483 0.3210 0.3995 -0.0009 0.0179  -0.0226 102 LYS   A NZ  
2153 N  N   A GLY   A 103 ? 0.3390 0.4573 0.2751 -0.0660 0.0018  0.0905  103 GLY   A N   
2154 N  N   B GLY   A 103 ? 0.3084 0.2801 0.2229 0.0161  -0.0008 0.0509  103 GLY   A N   
2155 C  CA  A GLY   A 103 ? 0.3438 0.4630 0.2720 -0.0537 0.0028  0.0722  103 GLY   A CA  
2156 C  CA  B GLY   A 103 ? 0.3070 0.2849 0.2244 0.0137  -0.0069 0.0567  103 GLY   A CA  
2157 C  C   A GLY   A 103 ? 0.3413 0.4676 0.2700 -0.0454 0.0118  0.0586  103 GLY   A C   
2158 C  C   B GLY   A 103 ? 0.2994 0.2841 0.2125 0.0090  -0.0064 0.0599  103 GLY   A C   
2159 O  O   A GLY   A 103 ? 0.3522 0.4753 0.2850 -0.0410 0.0119  0.0531  103 GLY   A O   
2160 O  O   B GLY   A 103 ? 0.3027 0.2827 0.2041 0.0050  -0.0072 0.0674  103 GLY   A O   
2167 N  N   A GLU   A 104 ? 0.3232 0.4594 0.2320 -0.0459 0.0221  0.0509  104 GLU   A N   
2168 N  N   B GLU   A 104 ? 0.2873 0.2838 0.2053 0.0099  -0.0132 0.0558  104 GLU   A N   
2169 C  CA  A GLU   A 104 ? 0.3022 0.4470 0.1985 -0.0520 0.0242  0.0424  104 GLU   A CA  
2170 C  CA  B GLU   A 104 ? 0.2780 0.2833 0.1943 0.0053  -0.0208 0.0448  104 GLU   A CA  
2171 C  C   A GLU   A 104 ? 0.3071 0.4542 0.1961 -0.0517 0.0164  0.0148  104 GLU   A C   
2172 C  C   B GLU   A 104 ? 0.2833 0.2890 0.2040 0.0087  -0.0176 0.0327  104 GLU   A C   
2173 O  O   A GLU   A 104 ? 0.3032 0.4587 0.2038 -0.0529 -0.0034 0.0104  104 GLU   A O   
2174 O  O   B GLU   A 104 ? 0.2811 0.2822 0.2038 0.0118  -0.0187 0.0393  104 GLU   A O   
2175 C  CB  A GLU   A 104 ? 0.2712 0.4273 0.1760 -0.0600 0.0327  0.0647  104 GLU   A CB  
2176 C  CB  B GLU   A 104 ? 0.2669 0.2804 0.1883 -0.0038 -0.0271 0.0433  104 GLU   A CB  
2177 C  CG  A GLU   A 104 ? 0.2486 0.4103 0.1740 -0.0633 0.0266  0.0782  104 GLU   A CG  
2178 C  CG  B GLU   A 104 ? 0.2623 0.2834 0.1964 -0.0123 -0.0357 0.0385  104 GLU   A CG  
2179 C  CD  A GLU   A 104 ? 0.2311 0.3927 0.1725 -0.0598 0.0246  0.0924  104 GLU   A CD  
2180 C  CD  B GLU   A 104 ? 0.2571 0.2846 0.1975 -0.0174 -0.0468 0.0363  104 GLU   A CD  
2181 O  OE1 A GLU   A 104 ? 0.2124 0.3754 0.1523 -0.0590 0.0156  0.0931  104 GLU   A OE1 
2182 O  OE1 B GLU   A 104 ? 0.2551 0.2855 0.1974 -0.0191 -0.0512 0.0339  104 GLU   A OE1 
2183 O  OE2 A GLU   A 104 ? 0.2432 0.3970 0.2041 -0.0633 0.0279  0.1042  104 GLU   A OE2 
2184 O  OE2 B GLU   A 104 ? 0.2596 0.2852 0.2076 -0.0210 -0.0473 0.0353  104 GLU   A OE2 
2197 N  N   A ASP   A 105 ? 0.3151 0.4553 0.2062 -0.0492 0.0265  -0.0127 105 ASP   A N   
2198 N  N   B ASP   A 105 ? 0.2954 0.3026 0.2301 0.0046  -0.0101 0.0135  105 ASP   A N   
2199 C  CA  A ASP   A 105 ? 0.3153 0.4544 0.2451 -0.0458 0.0385  -0.0384 105 ASP   A CA  
2200 C  CA  B ASP   A 105 ? 0.3045 0.3164 0.2630 0.0019  0.0006  -0.0100 105 ASP   A CA  
2201 C  C   A ASP   A 105 ? 0.2826 0.4330 0.2039 -0.0553 0.0350  -0.0580 105 ASP   A C   
2202 C  C   B ASP   A 105 ? 0.3019 0.3202 0.2516 -0.0074 0.0008  -0.0193 105 ASP   A C   
2203 O  O   A ASP   A 105 ? 0.2633 0.4281 0.1478 -0.0560 0.0429  -0.0838 105 ASP   A O   
2204 O  O   B ASP   A 105 ? 0.2965 0.3199 0.2279 -0.0063 0.0011  -0.0254 105 ASP   A O   
2205 C  CB  A ASP   A 105 ? 0.3445 0.4715 0.3146 -0.0335 0.0478  -0.0445 105 ASP   A CB  
2206 C  CB  B ASP   A 105 ? 0.3165 0.3258 0.3067 0.0080  0.0105  -0.0222 105 ASP   A CB  
2207 C  CG  A ASP   A 105 ? 0.3675 0.4857 0.3755 -0.0237 0.0508  -0.0530 105 ASP   A CG  
2208 C  CG  B ASP   A 105 ? 0.3265 0.3340 0.3464 0.0150  0.0170  -0.0322 105 ASP   A CG  
2209 O  OD1 A ASP   A 105 ? 0.3728 0.4924 0.3883 -0.0219 0.0496  -0.0644 105 ASP   A OD1 
2210 O  OD1 B ASP   A 105 ? 0.3282 0.3353 0.3512 0.0141  0.0163  -0.0375 105 ASP   A OD1 
2211 O  OD2 A ASP   A 105 ? 0.3772 0.4905 0.4110 -0.0222 0.0538  -0.0476 105 ASP   A OD2 
2212 O  OD2 B ASP   A 105 ? 0.3335 0.3386 0.3704 0.0180  0.0198  -0.0328 105 ASP   A OD2 
2221 N  N   A ILE   A 106 ? 0.2658 0.4201 0.2205 -0.0671 0.0110  -0.0583 106 ILE   A N   
2222 N  N   B ILE   A 106 ? 0.3028 0.3233 0.2624 -0.0168 -0.0030 -0.0212 106 ILE   A N   
2223 C  CA  A ILE   A 106 ? 0.2412 0.3989 0.2421 -0.0817 -0.0133 -0.0681 106 ILE   A CA  
2224 C  CA  B ILE   A 106 ? 0.3014 0.3258 0.2779 -0.0290 -0.0066 -0.0258 106 ILE   A CA  
2225 C  C   A ILE   A 106 ? 0.2267 0.3673 0.2437 -0.1013 -0.0064 -0.0869 106 ILE   A C   
2226 C  C   B ILE   A 106 ? 0.2976 0.3181 0.2790 -0.0375 0.0022  -0.0318 106 ILE   A C   
2227 O  O   A ILE   A 106 ? 0.2045 0.3529 0.2432 -0.1142 0.0136  -0.0865 106 ILE   A O   
2228 O  O   B ILE   A 106 ? 0.2946 0.3159 0.2759 -0.0375 0.0049  -0.0341 106 ILE   A O   
2229 C  CB  A ILE   A 106 ? 0.2412 0.4095 0.2740 -0.0665 -0.0359 -0.0425 106 ILE   A CB  
2230 C  CB  B ILE   A 106 ? 0.3052 0.3362 0.2987 -0.0302 -0.0176 -0.0179 106 ILE   A CB  
2231 C  CG1 A ILE   A 106 ? 0.2289 0.4084 0.3005 -0.0497 -0.0377 -0.0201 106 ILE   A CG1 
2232 C  CG1 B ILE   A 106 ? 0.3035 0.3393 0.3149 -0.0282 -0.0215 -0.0091 106 ILE   A CG1 
2233 C  CG2 A ILE   A 106 ? 0.2515 0.4155 0.2837 -0.0654 -0.0440 -0.0391 106 ILE   A CG2 
2234 C  CG2 B ILE   A 106 ? 0.3086 0.3400 0.3022 -0.0319 -0.0212 -0.0172 106 ILE   A CG2 
2235 C  CD1 A ILE   A 106 ? 0.2251 0.4044 0.3179 -0.0340 -0.0253 -0.0044 106 ILE   A CD1 
2236 C  CD1 B ILE   A 106 ? 0.3037 0.3389 0.3250 -0.0246 -0.0207 -0.0030 106 ILE   A CD1 
2259 N  N   A GLN   A 107 ? 0.2466 0.3508 0.2663 -0.0963 0.0033  -0.0979 107 GLN   A N   
2260 N  N   B GLN   A 107 ? 0.2972 0.3098 0.2896 -0.0446 0.0114  -0.0345 107 GLN   A N   
2261 C  CA  A GLN   A 107 ? 0.2766 0.3358 0.3402 -0.0806 0.0218  -0.0895 107 GLN   A CA  
2262 C  CA  B GLN   A 107 ? 0.2968 0.3022 0.3171 -0.0508 0.0208  -0.0358 107 GLN   A CA  
2263 C  C   A GLN   A 107 ? 0.2539 0.2855 0.3191 -0.0681 0.0509  -0.0674 107 GLN   A C   
2264 C  C   B GLN   A 107 ? 0.2638 0.2718 0.2951 -0.0563 0.0397  -0.0430 107 GLN   A C   
2265 O  O   A GLN   A 107 ? 0.2628 0.2767 0.3662 -0.0620 0.0679  -0.0744 107 GLN   A O   
2266 O  O   B GLN   A 107 ? 0.2687 0.2699 0.3114 -0.0575 0.0424  -0.0490 107 GLN   A O   
2267 C  CB  A GLN   A 107 ? 0.3192 0.3674 0.4330 -0.0830 0.0093  -0.0923 107 GLN   A CB  
2268 C  CB  B GLN   A 107 ? 0.3246 0.3233 0.3656 -0.0537 0.0090  -0.0264 107 GLN   A CB  
2269 C  CG  A GLN   A 107 ? 0.3637 0.3975 0.5308 -0.0779 -0.0008 -0.0857 107 GLN   A CG  
2270 C  CG  B GLN   A 107 ? 0.3493 0.3413 0.4181 -0.0546 -0.0021 -0.0146 107 GLN   A CG  
2271 C  CD  A GLN   A 107 ? 0.4046 0.4192 0.6143 -0.0732 -0.0075 -0.0763 107 GLN   A CD  
2272 C  CD  B GLN   A 107 ? 0.3703 0.3565 0.4641 -0.0534 -0.0109 -0.0020 107 GLN   A CD  
2273 O  OE1 A GLN   A 107 ? 0.4146 0.4266 0.6468 -0.0733 -0.0106 -0.0731 107 GLN   A OE1 
2274 O  OE1 B GLN   A 107 ? 0.3791 0.3622 0.4763 -0.0525 -0.0130 0.0043  107 GLN   A OE1 
2275 N  NE2 A GLN   A 107 ? 0.4103 0.4249 0.6410 -0.0713 -0.0112 -0.0763 107 GLN   A NE2 
2276 N  NE2 B GLN   A 107 ? 0.3756 0.3611 0.4766 -0.0533 -0.0172 0.0022  107 GLN   A NE2 
2293 N  N   . LEU   A 108 ? 0.2263 0.2429 0.2636 -0.0612 0.0474  -0.0533 108 LEU   A N   
2294 C  CA  . LEU   A 108 ? 0.1959 0.1949 0.2279 -0.0277 0.0426  -0.0217 108 LEU   A CA  
2295 C  C   . LEU   A 108 ? 0.1691 0.1469 0.2219 -0.0133 0.0361  -0.0016 108 LEU   A C   
2296 O  O   . LEU   A 108 ? 0.1638 0.1490 0.2350 -0.0024 0.0347  0.0004  108 LEU   A O   
2297 C  CB  . LEU   A 108 ? 0.1969 0.2049 0.2061 -0.0327 0.0438  -0.0184 108 LEU   A CB  
2298 C  CG  . LEU   A 108 ? 0.2085 0.2266 0.2305 -0.0265 0.0525  -0.0276 108 LEU   A CG  
2299 C  CD1 . LEU   A 108 ? 0.2275 0.2313 0.2403 -0.0345 0.0549  -0.0203 108 LEU   A CD1 
2300 C  CD2 . LEU   A 108 ? 0.2096 0.2483 0.2756 -0.0177 0.0470  -0.0208 108 LEU   A CD2 
2313 N  N   . LEU   A 109 ? 0.1527 0.1428 0.2146 0.0011  0.0246  0.0143  109 LEU   A N   
2314 C  CA  . LEU   A 109 ? 0.1482 0.1403 0.1970 0.0021  0.0121  0.0200  109 LEU   A CA  
2315 C  C   . LEU   A 109 ? 0.1384 0.1341 0.1903 -0.0099 0.0130  0.0120  109 LEU   A C   
2316 O  O   . LEU   A 109 ? 0.1469 0.1270 0.2043 -0.0027 0.0021  0.0045  109 LEU   A O   
2317 C  CB  . LEU   A 109 ? 0.1559 0.1433 0.2209 0.0157  0.0074  0.0305  109 LEU   A CB  
2318 C  CG  . LEU   A 109 ? 0.1517 0.1485 0.2240 0.0110  0.0128  0.0387  109 LEU   A CG  
2319 C  CD1 . LEU   A 109 ? 0.1561 0.1398 0.2359 0.0092  0.0257  0.0163  109 LEU   A CD1 
2320 C  CD2 . LEU   A 109 ? 0.1494 0.1660 0.2372 0.0054  0.0137  0.0346  109 LEU   A CD2 
2332 N  N   . LYS   A 110 ? 0.1436 0.1339 0.1803 -0.0098 0.0022  0.0055  110 LYS   A N   
2333 C  CA  . LYS   A 110 ? 0.1421 0.1258 0.1880 -0.0075 -0.0012 0.0118  110 LYS   A CA  
2334 C  C   . LYS   A 110 ? 0.1380 0.1244 0.1766 -0.0089 0.0080  -0.0067 110 LYS   A C   
2335 O  O   . LYS   A 110 ? 0.1308 0.1258 0.1946 -0.0072 0.0109  -0.0077 110 LYS   A O   
2336 C  CB  . LYS   A 110 ? 0.1446 0.1316 0.2121 -0.0077 -0.0051 -0.0024 110 LYS   A CB  
2337 C  CG  . LYS   A 110 ? 0.1530 0.1335 0.2214 -0.0012 -0.0071 -0.0043 110 LYS   A CG  
2338 C  CD  . LYS   A 110 ? 0.1512 0.1410 0.2407 -0.0101 -0.0003 -0.0043 110 LYS   A CD  
2339 C  CE  . LYS   A 110 ? 0.1582 0.1452 0.2519 -0.0097 0.0145  -0.0081 110 LYS   A CE  
2340 N  NZ  . LYS   A 110 ? 0.1606 0.1459 0.2641 -0.0197 0.0208  -0.0057 110 LYS   A NZ  
2354 N  N   . SER   A 111 ? 0.1379 0.1303 0.1810 0.0002  0.0074  0.0037  111 SER   A N   
2355 C  CA  . SER   A 111 ? 0.1317 0.1328 0.1870 -0.0032 0.0072  -0.0004 111 SER   A CA  
2356 C  C   . SER   A 111 ? 0.1301 0.1247 0.1906 -0.0099 0.0112  0.0079  111 SER   A C   
2357 O  O   . SER   A 111 ? 0.1414 0.1222 0.1975 -0.0033 0.0120  0.0051  111 SER   A O   
2358 C  CB  . SER   A 111 ? 0.1518 0.1551 0.1945 -0.0012 0.0149  -0.0066 111 SER   A CB  
2359 O  OG  . SER   A 111 ? 0.1951 0.1739 0.1999 0.0063  0.0248  -0.0176 111 SER   A OG  
2365 N  N   . ALA   A 112 ? 0.1354 0.1191 0.1926 -0.0050 0.0178  0.0058  112 ALA   A N   
2366 C  CA  . ALA   A 112 ? 0.1424 0.1198 0.1807 -0.0099 0.0199  0.0038  112 ALA   A CA  
2367 C  C   . ALA   A 112 ? 0.1293 0.1179 0.1845 -0.0010 0.0122  0.0055  112 ALA   A C   
2368 O  O   . ALA   A 112 ? 0.1305 0.1146 0.2028 -0.0131 0.0201  0.0089  112 ALA   A O   
2369 C  CB  . ALA   A 112 ? 0.1468 0.1220 0.1766 0.0012  0.0171  0.0092  112 ALA   A CB  
2375 N  N   . TYR   A 113 ? 0.1221 0.1235 0.1912 -0.0064 0.0122  0.0097  113 TYR   A N   
2376 C  CA  . TYR   A 113 ? 0.1210 0.1207 0.1825 -0.0053 0.0140  0.0170  113 TYR   A CA  
2377 C  C   . TYR   A 113 ? 0.1182 0.1210 0.1800 -0.0087 0.0111  0.0041  113 TYR   A C   
2378 O  O   . TYR   A 113 ? 0.1238 0.1222 0.1959 -0.0037 0.0134  0.0069  113 TYR   A O   
2379 C  CB  . TYR   A 113 ? 0.1159 0.1343 0.1966 -0.0055 0.0065  0.0192  113 TYR   A CB  
2380 C  CG  . TYR   A 113 ? 0.1225 0.1306 0.1819 -0.0106 0.0112  0.0228  113 TYR   A CG  
2381 C  CD1 . TYR   A 113 ? 0.1246 0.1341 0.1805 -0.0042 0.0041  0.0236  113 TYR   A CD1 
2382 C  CD2 . TYR   A 113 ? 0.1271 0.1325 0.1789 -0.0093 0.0019  0.0217  113 TYR   A CD2 
2383 C  CE1 . TYR   A 113 ? 0.1289 0.1459 0.1802 -0.0056 0.0070  0.0226  113 TYR   A CE1 
2384 C  CE2 . TYR   A 113 ? 0.1296 0.1472 0.1843 -0.0104 -0.0008 0.0269  113 TYR   A CE2 
2385 C  CZ  . TYR   A 113 ? 0.1245 0.1479 0.1811 0.0015  0.0095  0.0242  113 TYR   A CZ  
2386 O  OH  . TYR   A 113 ? 0.1258 0.1553 0.1945 0.0112  0.0097  0.0231  113 TYR   A OH  
2396 N  N   . GLU   A 114 ? 0.1202 0.1200 0.1899 -0.0054 0.0133  0.0176  114 GLU   A N   
2397 C  CA  . GLU   A 114 ? 0.1237 0.1170 0.2016 0.0025  0.0114  0.0144  114 GLU   A CA  
2398 C  C   . GLU   A 114 ? 0.1186 0.1229 0.1987 -0.0003 0.0087  0.0145  114 GLU   A C   
2399 O  O   . GLU   A 114 ? 0.1313 0.1244 0.2008 -0.0007 0.0082  0.0173  114 GLU   A O   
2400 C  CB  . GLU   A 114 ? 0.1253 0.1198 0.2039 -0.0050 0.0072  0.0130  114 GLU   A CB  
2401 C  CG  . GLU   A 114 ? 0.1394 0.1224 0.2054 0.0023  0.0145  0.0083  114 GLU   A CG  
2402 C  CD  . GLU   A 114 ? 0.1437 0.1245 0.2167 -0.0052 0.0087  0.0147  114 GLU   A CD  
2403 O  OE1 . GLU   A 114 ? 0.1477 0.1279 0.2129 -0.0088 0.0157  -0.0019 114 GLU   A OE1 
2404 O  OE2 . GLU   A 114 ? 0.1619 0.1316 0.2338 -0.0116 0.0108  -0.0049 114 GLU   A OE2 
2411 N  N   . ASN   A 115 ? 0.1260 0.1212 0.1807 -0.0099 0.0118  0.0052  115 ASN   A N   
2412 C  CA  . ASN   A 115 ? 0.1275 0.1262 0.1877 -0.0075 0.0120  0.0054  115 ASN   A CA  
2413 C  C   . ASN   A 115 ? 0.1278 0.1220 0.1846 -0.0124 0.0045  0.0092  115 ASN   A C   
2414 O  O   . ASN   A 115 ? 0.1268 0.1375 0.1880 -0.0104 0.0107  0.0236  115 ASN   A O   
2415 C  CB  . ASN   A 115 ? 0.1387 0.1329 0.1842 -0.0127 0.0125  0.0102  115 ASN   A CB  
2416 C  CG  . ASN   A 115 ? 0.1353 0.1499 0.1884 -0.0218 0.0227  0.0074  115 ASN   A CG  
2417 O  OD1 . ASN   A 115 ? 0.1368 0.2475 0.2252 -0.0155 0.0300  0.0229  115 ASN   A OD1 
2418 N  ND2 . ASN   A 115 ? 0.1422 0.1358 0.1857 -0.0114 0.0263  0.0114  115 ASN   A ND2 
2425 N  N   . PHE   A 116 ? 0.1203 0.1218 0.1908 -0.0021 0.0123  0.0171  116 PHE   A N   
2426 C  CA  . PHE   A 116 ? 0.1224 0.1338 0.1805 -0.0013 0.0184  0.0166  116 PHE   A CA  
2427 C  C   . PHE   A 116 ? 0.1220 0.1387 0.1872 -0.0055 0.0153  0.0245  116 PHE   A C   
2428 O  O   . PHE   A 116 ? 0.1287 0.1416 0.1978 0.0026  0.0139  0.0342  116 PHE   A O   
2429 C  CB  . PHE   A 116 ? 0.1214 0.1236 0.1982 -0.0004 0.0192  0.0213  116 PHE   A CB  
2430 C  CG  . PHE   A 116 ? 0.1258 0.1244 0.1783 -0.0083 0.0126  0.0121  116 PHE   A CG  
2431 C  CD1 . PHE   A 116 ? 0.1283 0.1220 0.1797 -0.0093 0.0096  0.0053  116 PHE   A CD1 
2432 C  CD2 . PHE   A 116 ? 0.1342 0.1296 0.1871 -0.0069 0.0167  0.0145  116 PHE   A CD2 
2433 C  CE1 . PHE   A 116 ? 0.1313 0.1205 0.1955 -0.0188 0.0074  0.0100  116 PHE   A CE1 
2434 C  CE2 . PHE   A 116 ? 0.1336 0.1260 0.1965 -0.0032 0.0163  0.0067  116 PHE   A CE2 
2435 C  CZ  . PHE   A 116 ? 0.1376 0.1154 0.1871 -0.0049 0.0074  0.0122  116 PHE   A CZ  
2445 N  N   . ASN   A 117 ? 0.1248 0.1313 0.1948 -0.0083 0.0177  0.0234  117 ASN   A N   
2446 C  CA  . ASN   A 117 ? 0.1267 0.1275 0.2048 -0.0075 0.0115  0.0293  117 ASN   A CA  
2447 C  C   . ASN   A 117 ? 0.1290 0.1369 0.2190 -0.0016 0.0146  0.0261  117 ASN   A C   
2448 O  O   . ASN   A 117 ? 0.1391 0.1448 0.2369 -0.0036 -0.0058 0.0437  117 ASN   A O   
2449 C  CB  . ASN   A 117 ? 0.1248 0.1384 0.2029 -0.0053 0.0076  0.0294  117 ASN   A CB  
2450 C  CG  . ASN   A 117 ? 0.1236 0.1363 0.2124 -0.0032 0.0135  0.0370  117 ASN   A CG  
2451 O  OD1 . ASN   A 117 ? 0.1228 0.1501 0.2254 -0.0093 0.0097  0.0243  117 ASN   A OD1 
2452 N  ND2 . ASN   A 117 ? 0.1231 0.1263 0.2147 -0.0041 0.0096  0.0293  117 ASN   A ND2 
2459 N  N   . GLN   A 118 ? 0.1289 0.1383 0.2176 -0.0102 0.0014  0.0298  118 GLN   A N   
2460 C  CA  . GLN   A 118 ? 0.1336 0.1528 0.2254 -0.0058 -0.0062 0.0263  118 GLN   A CA  
2461 C  C   . GLN   A 118 ? 0.1372 0.1592 0.2108 -0.0104 -0.0012 0.0370  118 GLN   A C   
2462 O  O   . GLN   A 118 ? 0.1334 0.1870 0.2285 -0.0043 -0.0085 0.0119  118 GLN   A O   
2463 C  CB  . GLN   A 118 ? 0.1271 0.1479 0.2358 -0.0034 0.0082  0.0317  118 GLN   A CB  
2464 C  CG  . GLN   A 118 ? 0.1267 0.1529 0.2354 -0.0055 0.0146  0.0337  118 GLN   A CG  
2465 C  CD  . GLN   A 118 ? 0.1271 0.1571 0.2465 -0.0012 0.0111  0.0294  118 GLN   A CD  
2466 O  OE1 . GLN   A 118 ? 0.1312 0.1667 0.2589 0.0084  0.0018  0.0177  118 GLN   A OE1 
2467 N  NE2 . GLN   A 118 ? 0.1352 0.1550 0.2478 0.0026  0.0071  0.0315  118 GLN   A NE2 
2476 N  N   . HIS   A 119 ? 0.1401 0.1558 0.1931 -0.0067 0.0047  0.0373  119 HIS   A N   
2477 C  CA  . HIS   A 119 ? 0.1452 0.1610 0.1964 -0.0075 -0.0030 0.0431  119 HIS   A CA  
2478 C  C   . HIS   A 119 ? 0.1565 0.1734 0.1871 -0.0101 0.0058  0.0391  119 HIS   A C   
2479 O  O   . HIS   A 119 ? 0.1578 0.1769 0.1935 -0.0241 -0.0056 0.0398  119 HIS   A O   
2480 C  CB  . HIS   A 119 ? 0.1512 0.1532 0.2246 -0.0034 0.0142  0.0437  119 HIS   A CB  
2481 C  CG  . HIS   A 119 ? 0.1466 0.1590 0.2617 0.0007  0.0091  0.0521  119 HIS   A CG  
2482 N  ND1 . HIS   A 119 ? 0.1634 0.1843 0.3203 -0.0114 0.0085  0.0338  119 HIS   A ND1 
2483 C  CD2 . HIS   A 119 ? 0.1565 0.1711 0.2783 0.0122  0.0235  0.0703  119 HIS   A CD2 
2484 C  CE1 . HIS   A 119 ? 0.1638 0.1815 0.3265 -0.0156 0.0248  0.0552  119 HIS   A CE1 
2485 N  NE2 . HIS   A 119 ? 0.1696 0.1786 0.3148 0.0035  0.0405  0.0741  119 HIS   A NE2 
2493 N  N   . GLU   A 120 ? 0.1611 0.1978 0.1988 -0.0095 -0.0017 0.0668  120 GLU   A N   
2494 C  CA  . GLU   A 120 ? 0.1823 0.2295 0.2331 0.0023  -0.0071 0.1062  120 GLU   A CA  
2495 C  C   . GLU   A 120 ? 0.1625 0.2128 0.2059 -0.0099 -0.0039 0.0991  120 GLU   A C   
2496 O  O   . GLU   A 120 ? 0.1620 0.2030 0.2183 -0.0166 0.0007  0.0887  120 GLU   A O   
2497 C  CB  . GLU   A 120 ? 0.2524 0.2955 0.2912 0.0233  -0.0076 0.1509  120 GLU   A CB  
2498 C  CG  . GLU   A 120 ? 0.3543 0.3733 0.4034 0.0368  -0.0026 0.1557  120 GLU   A CG  
2499 C  CD  . GLU   A 120 ? 0.4457 0.4479 0.5260 0.0458  0.0109  0.1379  120 GLU   A CD  
2500 O  OE1 . GLU   A 120 ? 0.4704 0.4586 0.5486 0.0469  0.0146  0.1327  120 GLU   A OE1 
2501 O  OE2 . GLU   A 120 ? 0.4867 0.4842 0.5757 0.0476  0.0165  0.1302  120 GLU   A OE2 
2508 N  N   . VAL   A 121 ? 0.1591 0.2116 0.1779 -0.0112 0.0035  0.0753  121 VAL   A N   
2509 C  CA  . VAL   A 121 ? 0.1687 0.2185 0.1659 -0.0151 0.0088  0.0714  121 VAL   A CA  
2510 C  C   . VAL   A 121 ? 0.1583 0.1977 0.1486 -0.0230 0.0049  0.0519  121 VAL   A C   
2511 O  O   . VAL   A 121 ? 0.1631 0.1958 0.1735 -0.0294 -0.0077 0.0443  121 VAL   A O   
2512 C  CB  . VAL   A 121 ? 0.2075 0.2574 0.2038 -0.0014 0.0151  0.0786  121 VAL   A CB  
2513 C  CG1 . VAL   A 121 ? 0.2099 0.2706 0.2055 0.0034  0.0241  0.0839  121 VAL   A CG1 
2514 C  CG2 . VAL   A 121 ? 0.2298 0.2750 0.2487 -0.0109 0.0167  0.0637  121 VAL   A CG2 
2524 N  N   . LEU   A 122 ? 0.1466 0.1726 0.1614 -0.0219 -0.0016 0.0434  122 LEU   A N   
2525 C  CA  . LEU   A 122 ? 0.1531 0.1542 0.1677 -0.0182 0.0131  0.0404  122 LEU   A CA  
2526 C  C   . LEU   A 122 ? 0.1461 0.1538 0.1691 -0.0259 0.0042  0.0361  122 LEU   A C   
2527 O  O   . LEU   A 122 ? 0.1481 0.1601 0.1911 -0.0243 0.0034  0.0427  122 LEU   A O   
2528 C  CB  . LEU   A 122 ? 0.1695 0.1576 0.1927 -0.0067 0.0091  0.0494  122 LEU   A CB  
2529 C  CG  . LEU   A 122 ? 0.1681 0.1616 0.1855 -0.0099 0.0217  0.0367  122 LEU   A CG  
2530 C  CD1 . LEU   A 122 ? 0.1873 0.1657 0.2039 -0.0138 0.0348  0.0317  122 LEU   A CD1 
2531 C  CD2 . LEU   A 122 ? 0.1635 0.1573 0.1809 -0.0070 0.0255  0.0262  122 LEU   A CD2 
2543 N  N   . LEU   A 123 ? 0.1356 0.1527 0.1716 -0.0239 -0.0001 0.0321  123 LEU   A N   
2544 C  CA  . LEU   A 123 ? 0.1363 0.1530 0.1595 -0.0261 0.0039  0.0300  123 LEU   A CA  
2545 C  C   . LEU   A 123 ? 0.1368 0.1493 0.1421 -0.0223 0.0042  0.0350  123 LEU   A C   
2546 O  O   . LEU   A 123 ? 0.1324 0.1599 0.1596 -0.0240 0.0041  0.0392  123 LEU   A O   
2547 C  CB  . LEU   A 123 ? 0.1499 0.1614 0.1532 -0.0247 0.0137  0.0264  123 LEU   A CB  
2548 C  CG  . LEU   A 123 ? 0.1506 0.1771 0.1640 -0.0187 0.0137  0.0204  123 LEU   A CG  
2549 C  CD1 . LEU   A 123 ? 0.1599 0.1828 0.1697 -0.0057 0.0097  0.0166  123 LEU   A CD1 
2550 C  CD2 . LEU   A 123 ? 0.1662 0.1820 0.1734 -0.0148 0.0030  0.0172  123 LEU   A CD2 
2562 N  N   . ALA   A 124 ? 0.1335 0.1422 0.1346 -0.0159 0.0078  0.0325  124 ALA   A N   
2563 C  CA  . ALA   A 124 ? 0.1325 0.1392 0.1455 -0.0115 -0.0026 0.0230  124 ALA   A CA  
2564 C  C   . ALA   A 124 ? 0.1253 0.1345 0.1470 -0.0140 0.0087  0.0251  124 ALA   A C   
2565 O  O   . ALA   A 124 ? 0.1264 0.1431 0.1701 -0.0128 0.0145  0.0328  124 ALA   A O   
2566 C  CB  . ALA   A 124 ? 0.1317 0.1318 0.1698 -0.0044 0.0045  0.0235  124 ALA   A CB  
2572 N  N   A PRO   A 125 ? 0.1168 0.1327 0.1558 -0.0150 0.0053  0.0328  125 PRO   A N   
2573 N  N   B PRO   A 125 ? 0.1330 0.1421 0.1337 -0.0137 0.0076  0.0248  125 PRO   A N   
2574 C  CA  A PRO   A 125 ? 0.1234 0.1297 0.1531 -0.0034 0.0083  0.0229  125 PRO   A CA  
2575 C  CA  B PRO   A 125 ? 0.1409 0.1439 0.1314 -0.0077 0.0053  0.0154  125 PRO   A CA  
2576 C  C   A PRO   A 125 ? 0.1145 0.1280 0.1515 -0.0064 0.0049  0.0257  125 PRO   A C   
2577 C  C   B PRO   A 125 ? 0.1347 0.1439 0.1290 0.0005  0.0065  0.0161  125 PRO   A C   
2578 O  O   A PRO   A 125 ? 0.1200 0.1277 0.1592 0.0016  0.0028  0.0170  125 PRO   A O   
2579 O  O   B PRO   A 125 ? 0.1405 0.1485 0.1437 0.0017  0.0101  0.0191  125 PRO   A O   
2580 C  CB  A PRO   A 125 ? 0.1314 0.1259 0.1532 -0.0093 0.0108  0.0217  125 PRO   A CB  
2581 C  CB  B PRO   A 125 ? 0.1460 0.1445 0.1308 -0.0109 0.0087  0.0125  125 PRO   A CB  
2582 C  CG  A PRO   A 125 ? 0.1265 0.1210 0.1537 -0.0060 0.0129  0.0252  125 PRO   A CG  
2583 C  CG  B PRO   A 125 ? 0.1495 0.1457 0.1312 -0.0136 0.0043  0.0123  125 PRO   A CG  
2584 C  CD  A PRO   A 125 ? 0.1208 0.1336 0.1611 -0.0152 0.0099  0.0290  125 PRO   A CD  
2585 C  CD  B PRO   A 125 ? 0.1405 0.1501 0.1332 -0.0153 0.0097  0.0188  125 PRO   A CD  
2600 N  N   A LEU   A 126 ? 0.1135 0.1308 0.1690 -0.0007 0.0066  0.0214  126 LEU   A N   
2601 N  N   B LEU   A 126 ? 0.1383 0.1406 0.1332 -0.0013 -0.0008 0.0115  126 LEU   A N   
2602 C  CA  A LEU   A 126 ? 0.1197 0.1343 0.1833 -0.0028 0.0081  0.0221  126 LEU   A CA  
2603 C  CA  B LEU   A 126 ? 0.1317 0.1312 0.1345 0.0018  0.0096  0.0102  126 LEU   A CA  
2604 C  C   A LEU   A 126 ? 0.1274 0.1316 0.1852 -0.0009 0.0049  0.0149  126 LEU   A C   
2605 C  C   B LEU   A 126 ? 0.1291 0.1237 0.1435 0.0052  0.0198  0.0114  126 LEU   A C   
2606 O  O   A LEU   A 126 ? 0.1443 0.1296 0.1979 0.0071  0.0185  0.0180  126 LEU   A O   
2607 O  O   B LEU   A 126 ? 0.1428 0.1191 0.1577 0.0091  0.0283  0.0214  126 LEU   A O   
2608 C  CB  A LEU   A 126 ? 0.1251 0.1308 0.1874 0.0014  0.0055  0.0160  126 LEU   A CB  
2609 C  CB  B LEU   A 126 ? 0.1360 0.1385 0.1518 -0.0055 0.0115  0.0011  126 LEU   A CB  
2610 C  CG  A LEU   A 126 ? 0.1250 0.1364 0.2094 0.0022  0.0094  0.0111  126 LEU   A CG  
2611 C  CG  B LEU   A 126 ? 0.1322 0.1359 0.1626 -0.0011 0.0119  -0.0050 126 LEU   A CG  
2612 C  CD1 A LEU   A 126 ? 0.1348 0.1470 0.2445 0.0012  0.0099  0.0184  126 LEU   A CD1 
2613 C  CD1 B LEU   A 126 ? 0.1363 0.1365 0.1779 0.0024  0.0038  -0.0124 126 LEU   A CD1 
2614 C  CD2 A LEU   A 126 ? 0.1331 0.1336 0.1999 -0.0028 0.0091  0.0061  126 LEU   A CD2 
2615 C  CD2 B LEU   A 126 ? 0.1267 0.1355 0.1678 -0.0010 0.0092  -0.0017 126 LEU   A CD2 
2638 N  N   A LEU   A 127 ? 0.1279 0.1352 0.1750 0.0025  0.0015  0.0127  127 LEU   A N   
2639 N  N   B LEU   A 127 ? 0.1243 0.1281 0.1398 0.0012  0.0152  0.0137  127 LEU   A N   
2640 C  CA  A LEU   A 127 ? 0.1278 0.1356 0.1639 -0.0025 -0.0016 0.0076  127 LEU   A CA  
2641 C  CA  B LEU   A 127 ? 0.1227 0.1333 0.1436 0.0035  0.0121  0.0208  127 LEU   A CA  
2642 C  C   A LEU   A 127 ? 0.1268 0.1282 0.1516 -0.0010 -0.0073 0.0081  127 LEU   A C   
2643 C  C   B LEU   A 127 ? 0.1258 0.1349 0.1493 -0.0002 0.0078  0.0151  127 LEU   A C   
2644 O  O   A LEU   A 127 ? 0.1354 0.1261 0.1523 -0.0154 -0.0099 0.0125  127 LEU   A O   
2645 O  O   B LEU   A 127 ? 0.1332 0.1388 0.1544 -0.0090 0.0212  0.0214  127 LEU   A O   
2646 C  CB  A LEU   A 127 ? 0.1355 0.1416 0.1633 0.0079  0.0088  0.0144  127 LEU   A CB  
2647 C  CB  B LEU   A 127 ? 0.1231 0.1425 0.1425 0.0044  0.0033  0.0170  127 LEU   A CB  
2648 C  CG  A LEU   A 127 ? 0.1379 0.1449 0.1703 0.0094  -0.0003 0.0184  127 LEU   A CG  
2649 C  CG  B LEU   A 127 ? 0.1266 0.1516 0.1454 0.0115  -0.0116 0.0171  127 LEU   A CG  
2650 C  CD1 A LEU   A 127 ? 0.1416 0.1406 0.1838 0.0034  0.0082  0.0096  127 LEU   A CD1 
2651 C  CD1 B LEU   A 127 ? 0.1233 0.1536 0.1593 0.0202  -0.0063 0.0212  127 LEU   A CD1 
2652 C  CD2 A LEU   A 127 ? 0.1497 0.1474 0.1857 0.0168  -0.0127 0.0156  127 LEU   A CD2 
2653 C  CD2 B LEU   A 127 ? 0.1364 0.1604 0.1468 0.0094  -0.0262 0.0080  127 LEU   A CD2 
2676 N  N   A SER   A 128 ? 0.1351 0.1269 0.1548 -0.0056 -0.0059 0.0129  128 SER   A N   
2677 N  N   B SER   A 128 ? 0.1282 0.1366 0.1544 -0.0050 -0.0041 0.0192  128 SER   A N   
2678 C  CA  A SER   A 128 ? 0.1517 0.1378 0.1464 -0.0059 0.0016  0.0180  128 SER   A CA  
2679 C  CA  B SER   A 128 ? 0.1300 0.1390 0.1440 -0.0052 -0.0163 0.0200  128 SER   A CA  
2680 C  C   A SER   A 128 ? 0.1588 0.1424 0.1527 -0.0023 0.0070  0.0239  128 SER   A C   
2681 C  C   B SER   A 128 ? 0.1337 0.1352 0.1441 -0.0087 -0.0327 0.0304  128 SER   A C   
2682 O  O   A SER   A 128 ? 0.1721 0.1573 0.1645 -0.0004 0.0165  0.0130  128 SER   A O   
2683 O  O   B SER   A 128 ? 0.1309 0.1383 0.1479 -0.0069 -0.0443 0.0244  128 SER   A O   
2684 C  CB  A SER   A 128 ? 0.1504 0.1523 0.1504 -0.0066 0.0018  0.0212  128 SER   A CB  
2685 C  CB  B SER   A 128 ? 0.1270 0.1457 0.1363 -0.0041 -0.0179 0.0130  128 SER   A CB  
2686 O  OG  A SER   A 128 ? 0.1537 0.1630 0.1587 -0.0102 0.0100  0.0160  128 SER   A OG  
2687 O  OG  B SER   A 128 ? 0.1260 0.1528 0.1488 -0.0081 -0.0117 0.0078  128 SER   A OG  
2698 N  N   A ALA   A 129 ? 0.1450 0.1476 0.1765 -0.0051 0.0029  0.0345  129 ALA   A N   
2699 N  N   B ALA   A 129 ? 0.1369 0.1384 0.1555 -0.0078 -0.0334 0.0391  129 ALA   A N   
2700 C  CA  A ALA   A 129 ? 0.1311 0.1504 0.1854 0.0001  0.0003  0.0345  129 ALA   A CA  
2701 C  CA  B ALA   A 129 ? 0.1424 0.1439 0.1621 -0.0061 -0.0266 0.0410  129 ALA   A CA  
2702 C  C   A ALA   A 129 ? 0.1401 0.1509 0.1624 -0.0022 -0.0062 0.0136  129 ALA   A C   
2703 C  C   B ALA   A 129 ? 0.1535 0.1492 0.1650 -0.0117 -0.0280 0.0338  129 ALA   A C   
2704 O  O   A ALA   A 129 ? 0.1492 0.1579 0.1646 -0.0069 -0.0085 0.0242  129 ALA   A O   
2705 O  O   B ALA   A 129 ? 0.1549 0.1505 0.1611 -0.0147 -0.0270 0.0347  129 ALA   A O   
2706 C  CB  A ALA   A 129 ? 0.1365 0.1710 0.2029 0.0079  0.0003  0.0472  129 ALA   A CB  
2707 C  CB  B ALA   A 129 ? 0.1462 0.1559 0.1679 -0.0016 -0.0243 0.0420  129 ALA   A CB  
2718 N  N   A GLY   A 130 ? 0.1391 0.1430 0.1553 -0.0008 0.0000  0.0141  130 GLY   A N   
2719 N  N   B GLY   A 130 ? 0.1627 0.1533 0.1723 -0.0134 -0.0262 0.0357  130 GLY   A N   
2720 C  CA  A GLY   A 130 ? 0.1633 0.1392 0.1623 0.0036  0.0008  0.0117  130 GLY   A CA  
2721 C  CA  B GLY   A 130 ? 0.1732 0.1543 0.1806 -0.0141 -0.0273 0.0251  130 GLY   A CA  
2722 C  C   A GLY   A 130 ? 0.1683 0.1356 0.1415 0.0044  -0.0014 0.0133  130 GLY   A C   
2723 C  C   B GLY   A 130 ? 0.1773 0.1551 0.1781 -0.0159 -0.0350 0.0243  130 GLY   A C   
2724 O  O   A GLY   A 130 ? 0.1722 0.1320 0.1409 -0.0016 -0.0044 0.0162  130 GLY   A O   
2725 O  O   B GLY   A 130 ? 0.1852 0.1561 0.1907 -0.0154 -0.0340 0.0322  130 GLY   A O   
2732 N  N   A ILE   A 131 ? 0.1810 0.1375 0.1563 -0.0051 -0.0093 0.0166  131 ILE   A N   
2733 N  N   B ILE   A 131 ? 0.1745 0.1495 0.1722 -0.0152 -0.0404 0.0264  131 ILE   A N   
2734 C  CA  A ILE   A 131 ? 0.1911 0.1416 0.1513 -0.0123 -0.0231 0.0146  131 ILE   A CA  
2735 C  CA  B ILE   A 131 ? 0.1779 0.1446 0.1691 -0.0092 -0.0441 0.0228  131 ILE   A CA  
2736 C  C   A ILE   A 131 ? 0.1813 0.1486 0.1490 -0.0125 -0.0130 0.0278  131 ILE   A C   
2737 C  C   B ILE   A 131 ? 0.1770 0.1470 0.1581 -0.0070 -0.0446 0.0233  131 ILE   A C   
2738 O  O   A ILE   A 131 ? 0.1966 0.1573 0.1644 -0.0042 -0.0142 0.0317  131 ILE   A O   
2739 O  O   B ILE   A 131 ? 0.1872 0.1464 0.1641 -0.0066 -0.0376 0.0223  131 ILE   A O   
2740 C  CB  A ILE   A 131 ? 0.2075 0.1553 0.1573 -0.0214 -0.0361 0.0012  131 ILE   A CB  
2741 C  CB  B ILE   A 131 ? 0.1803 0.1495 0.1791 -0.0003 -0.0536 0.0151  131 ILE   A CB  
2742 C  CG1 A ILE   A 131 ? 0.2114 0.1872 0.1708 -0.0263 -0.0468 0.0026  131 ILE   A CG1 
2743 C  CG1 B ILE   A 131 ? 0.1866 0.1623 0.1812 0.0079  -0.0530 0.0105  131 ILE   A CG1 
2744 C  CG2 A ILE   A 131 ? 0.2152 0.1464 0.1765 -0.0173 -0.0330 -0.0102 131 ILE   A CG2 
2745 C  CG2 B ILE   A 131 ? 0.1765 0.1499 0.1859 0.0016  -0.0558 0.0140  131 ILE   A CG2 
2746 C  CD1 A ILE   A 131 ? 0.2143 0.1967 0.2036 -0.0335 -0.0491 -0.0015 131 ILE   A CD1 
2747 C  CD1 B ILE   A 131 ? 0.1917 0.1633 0.1776 0.0079  -0.0560 0.0066  131 ILE   A CD1 
2770 N  N   A PHE   A 132 ? 0.1696 0.1452 0.1656 -0.0121 -0.0065 0.0256  132 PHE   A N   
2771 N  N   B PHE   A 132 ? 0.1695 0.1488 0.1596 0.0003  -0.0423 0.0183  132 PHE   A N   
2772 C  CA  A PHE   A 132 ? 0.1720 0.1515 0.1612 -0.0161 -0.0052 0.0135  132 PHE   A CA  
2773 C  CA  B PHE   A 132 ? 0.1694 0.1520 0.1632 -0.0053 -0.0310 0.0127  132 PHE   A CA  
2774 C  C   A PHE   A 132 ? 0.1696 0.1625 0.1547 -0.0156 -0.0111 0.0145  132 PHE   A C   
2775 C  C   B PHE   A 132 ? 0.1766 0.1689 0.1712 -0.0048 -0.0290 0.0156  132 PHE   A C   
2776 O  O   A PHE   A 132 ? 0.1734 0.1671 0.1621 -0.0273 -0.0035 0.0210  132 PHE   A O   
2777 O  O   B PHE   A 132 ? 0.1861 0.1803 0.1694 -0.0109 -0.0194 0.0241  132 PHE   A O   
2778 C  CB  A PHE   A 132 ? 0.1699 0.1464 0.1549 -0.0089 -0.0113 0.0247  132 PHE   A CB  
2779 C  CB  B PHE   A 132 ? 0.1630 0.1433 0.1462 -0.0064 -0.0220 0.0182  132 PHE   A CB  
2780 C  CG  A PHE   A 132 ? 0.1675 0.1428 0.1521 -0.0014 -0.0169 0.0259  132 PHE   A CG  
2781 C  CG  B PHE   A 132 ? 0.1602 0.1417 0.1387 -0.0060 -0.0206 0.0020  132 PHE   A CG  
2782 C  CD1 A PHE   A 132 ? 0.1677 0.1521 0.1643 0.0029  -0.0134 0.0138  132 PHE   A CD1 
2783 C  CD1 B PHE   A 132 ? 0.1602 0.1504 0.1478 -0.0017 -0.0116 -0.0095 132 PHE   A CD1 
2784 C  CD2 A PHE   A 132 ? 0.1684 0.1435 0.1642 -0.0092 -0.0149 0.0194  132 PHE   A CD2 
2785 C  CD2 B PHE   A 132 ? 0.1619 0.1398 0.1443 -0.0047 -0.0175 -0.0153 132 PHE   A CD2 
2786 C  CE1 A PHE   A 132 ? 0.1654 0.1561 0.1711 0.0002  -0.0152 0.0001  132 PHE   A CE1 
2787 C  CE1 B PHE   A 132 ? 0.1578 0.1539 0.1488 -0.0009 -0.0084 -0.0152 132 PHE   A CE1 
2788 C  CE2 A PHE   A 132 ? 0.1658 0.1445 0.1728 -0.0021 -0.0246 0.0100  132 PHE   A CE2 
2789 C  CE2 B PHE   A 132 ? 0.1575 0.1467 0.1465 -0.0008 -0.0172 -0.0191 132 PHE   A CE2 
2790 C  CZ  A PHE   A 132 ? 0.1631 0.1518 0.1777 -0.0073 -0.0302 -0.0016 132 PHE   A CZ  
2791 C  CZ  B PHE   A 132 ? 0.1551 0.1504 0.1470 -0.0025 -0.0119 -0.0216 132 PHE   A CZ  
2810 N  N   A GLY   A 133 ? 0.1721 0.1679 0.1454 -0.0111 -0.0260 0.0256  133 GLY   A N   
2811 N  N   B GLY   A 133 ? 0.1781 0.1732 0.1691 -0.0022 -0.0320 0.0132  133 GLY   A N   
2812 C  CA  A GLY   A 133 ? 0.1833 0.1801 0.1589 -0.0153 -0.0317 0.0171  133 GLY   A CA  
2813 C  CA  B GLY   A 133 ? 0.1785 0.1779 0.1703 0.0026  -0.0310 0.0088  133 GLY   A CA  
2814 C  C   A GLY   A 133 ? 0.1939 0.1870 0.1653 -0.0143 -0.0430 0.0018  133 GLY   A C   
2815 C  C   B GLY   A 133 ? 0.1786 0.1824 0.1709 0.0104  -0.0325 -0.0037 133 GLY   A C   
2816 O  O   A GLY   A 133 ? 0.2075 0.2014 0.1673 -0.0101 -0.0324 -0.0187 133 GLY   A O   
2817 O  O   B GLY   A 133 ? 0.1827 0.1882 0.1627 0.0174  -0.0343 -0.0204 133 GLY   A O   
2824 N  N   A ALA   A 134 ? 0.1944 0.1705 0.1663 -0.0219 -0.0380 0.0033  134 ALA   A N   
2825 N  N   B ALA   A 134 ? 0.1775 0.1777 0.1761 0.0081  -0.0247 -0.0040 134 ALA   A N   
2826 C  CA  A ALA   A 134 ? 0.1910 0.1717 0.1952 -0.0213 -0.0379 -0.0007 134 ALA   A CA  
2827 C  CA  B ALA   A 134 ? 0.1724 0.1744 0.1837 0.0082  -0.0184 -0.0085 134 ALA   A CA  
2828 C  C   A ALA   A 134 ? 0.1955 0.1717 0.1895 -0.0175 -0.0390 0.0030  134 ALA   A C   
2829 C  C   B ALA   A 134 ? 0.1731 0.1663 0.1784 0.0068  -0.0153 -0.0121 134 ALA   A C   
2830 O  O   A ALA   A 134 ? 0.2125 0.1781 0.1989 -0.0243 -0.0273 0.0028  134 ALA   A O   
2831 O  O   B ALA   A 134 ? 0.1754 0.1635 0.1870 0.0037  0.0005  -0.0198 134 ALA   A O   
2832 C  CB  A ALA   A 134 ? 0.1993 0.1707 0.2272 -0.0189 -0.0363 -0.0072 134 ALA   A CB  
2833 C  CB  B ALA   A 134 ? 0.1746 0.1765 0.2003 0.0093  -0.0165 -0.0084 134 ALA   A CB  
2844 N  N   A ASP   A 135 ? 0.1940 0.1665 0.1999 -0.0117 -0.0337 0.0084  135 ASP   A N   
2845 N  N   B ASP   A 135 ? 0.1812 0.1679 0.1820 -0.0005 -0.0224 -0.0038 135 ASP   A N   
2846 C  CA  A ASP   A 135 ? 0.1923 0.1750 0.2206 -0.0148 -0.0409 0.0117  135 ASP   A CA  
2847 C  CA  B ASP   A 135 ? 0.1835 0.1684 0.1923 -0.0046 -0.0259 -0.0061 135 ASP   A CA  
2848 C  C   A ASP   A 135 ? 0.1769 0.1614 0.2226 -0.0136 -0.0283 0.0251  135 ASP   A C   
2849 C  C   B ASP   A 135 ? 0.1706 0.1574 0.1873 0.0002  -0.0201 -0.0080 135 ASP   A C   
2850 O  O   A ASP   A 135 ? 0.1693 0.1548 0.2317 -0.0073 -0.0276 0.0330  135 ASP   A O   
2851 O  O   B ASP   A 135 ? 0.1667 0.1540 0.1838 0.0050  -0.0186 -0.0016 135 ASP   A O   
2852 C  CB  A ASP   A 135 ? 0.2152 0.2009 0.2503 -0.0263 -0.0548 -0.0009 135 ASP   A CB  
2853 C  CB  B ASP   A 135 ? 0.1982 0.1842 0.2058 -0.0091 -0.0328 -0.0082 135 ASP   A CB  
2854 C  CG  A ASP   A 135 ? 0.2298 0.2221 0.2826 -0.0467 -0.0612 -0.0022 135 ASP   A CG  
2855 C  CG  B ASP   A 135 ? 0.2066 0.1995 0.2246 -0.0114 -0.0359 -0.0088 135 ASP   A CG  
2856 O  OD1 A ASP   A 135 ? 0.2141 0.2295 0.2898 -0.0608 -0.0707 0.0183  135 ASP   A OD1 
2857 O  OD1 B ASP   A 135 ? 0.2078 0.1986 0.2409 -0.0111 -0.0315 -0.0073 135 ASP   A OD1 
2858 O  OD2 A ASP   A 135 ? 0.2611 0.2431 0.3247 -0.0508 -0.0402 -0.0092 135 ASP   A OD2 
2859 O  OD2 B ASP   A 135 ? 0.2110 0.2099 0.2393 -0.0121 -0.0422 -0.0085 135 ASP   A OD2 
2868 N  N   A PRO   A 136 ? 0.1611 0.1542 0.2309 -0.0064 -0.0210 0.0298  136 PRO   A N   
2869 N  N   B PRO   A 136 ? 0.1615 0.1503 0.1853 0.0008  -0.0106 -0.0187 136 PRO   A N   
2870 C  CA  A PRO   A 136 ? 0.1538 0.1525 0.2453 -0.0085 -0.0186 0.0127  136 PRO   A CA  
2871 C  CA  B PRO   A 136 ? 0.1579 0.1570 0.1835 -0.0018 0.0037  -0.0273 136 PRO   A CA  
2872 C  C   A PRO   A 136 ? 0.1342 0.1469 0.2445 0.0008  -0.0170 0.0085  136 PRO   A C   
2873 C  C   B PRO   A 136 ? 0.1474 0.1619 0.1739 0.0030  0.0086  -0.0188 136 PRO   A C   
2874 O  O   A PRO   A 136 ? 0.1303 0.1556 0.2272 -0.0047 -0.0089 0.0066  136 PRO   A O   
2875 O  O   B PRO   A 136 ? 0.1418 0.1559 0.1506 0.0109  0.0284  -0.0185 136 PRO   A O   
2876 C  CB  A PRO   A 136 ? 0.1682 0.1532 0.2528 -0.0101 -0.0176 0.0174  136 PRO   A CB  
2877 C  CB  B PRO   A 136 ? 0.1676 0.1551 0.1940 -0.0000 0.0023  -0.0297 136 PRO   A CB  
2878 C  CG  A PRO   A 136 ? 0.1765 0.1581 0.2588 -0.0042 -0.0183 0.0191  136 PRO   A CG  
2879 C  CG  B PRO   A 136 ? 0.1725 0.1503 0.2025 0.0017  -0.0034 -0.0280 136 PRO   A CG  
2880 C  CD  A PRO   A 136 ? 0.1727 0.1539 0.2436 -0.0014 -0.0189 0.0268  136 PRO   A CD  
2881 C  CD  B PRO   A 136 ? 0.1661 0.1452 0.1949 0.0039  -0.0045 -0.0182 136 PRO   A CD  
2896 N  N   A ILE   A 137 ? 0.1330 0.1436 0.2454 0.0019  -0.0217 0.0183  137 ILE   A N   
2897 N  N   B ILE   A 137 ? 0.1495 0.1642 0.1864 -0.0006 0.0032  -0.0136 137 ILE   A N   
2898 C  CA  A ILE   A 137 ? 0.1366 0.1547 0.2423 -0.0105 -0.0268 0.0208  137 ILE   A CA  
2899 C  CA  B ILE   A 137 ? 0.1530 0.1715 0.1906 -0.0000 0.0051  -0.0131 137 ILE   A CA  
2900 C  C   A ILE   A 137 ? 0.1400 0.1571 0.2282 -0.0159 -0.0252 0.0262  137 ILE   A C   
2901 C  C   B ILE   A 137 ? 0.1488 0.1761 0.1886 -0.0047 0.0108  -0.0070 137 ILE   A C   
2902 O  O   A ILE   A 137 ? 0.1466 0.1512 0.2344 -0.0161 -0.0134 0.0221  137 ILE   A O   
2903 O  O   B ILE   A 137 ? 0.1450 0.1757 0.1926 -0.0041 0.0152  -0.0078 137 ILE   A O   
2904 C  CB  A ILE   A 137 ? 0.1438 0.1652 0.2606 -0.0136 -0.0377 0.0231  137 ILE   A CB  
2905 C  CB  B ILE   A 137 ? 0.1624 0.1724 0.2073 0.0023  -0.0079 -0.0116 137 ILE   A CB  
2906 C  CG1 A ILE   A 137 ? 0.1519 0.1838 0.2996 -0.0162 -0.0348 0.0369  137 ILE   A CG1 
2907 C  CG1 B ILE   A 137 ? 0.1730 0.1779 0.2353 0.0057  -0.0236 -0.0045 137 ILE   A CG1 
2908 C  CG2 A ILE   A 137 ? 0.1554 0.1703 0.2684 -0.0150 -0.0337 0.0051  137 ILE   A CG2 
2909 C  CG2 B ILE   A 137 ? 0.1669 0.1691 0.2078 0.0069  -0.0106 -0.0177 137 ILE   A CG2 
2910 C  CD1 A ILE   A 137 ? 0.1704 0.2012 0.3237 -0.0125 -0.0276 0.0397  137 ILE   A CD1 
2911 C  CD1 B ILE   A 137 ? 0.1817 0.1789 0.2535 0.0063  -0.0324 0.0060  137 ILE   A CD1 
2934 N  N   A HIS   A 138 ? 0.1432 0.1749 0.2228 -0.0119 -0.0169 0.0226  138 HIS   A N   
2935 N  N   B HIS   A 138 ? 0.1480 0.1852 0.1866 -0.0078 0.0166  -0.0048 138 HIS   A N   
2936 C  CA  A HIS   A 138 ? 0.1418 0.1878 0.2142 -0.0140 -0.0086 0.0233  138 HIS   A CA  
2937 C  CA  B HIS   A 138 ? 0.1460 0.1828 0.1842 -0.0089 0.0148  0.0020  138 HIS   A CA  
2938 C  C   A HIS   A 138 ? 0.1350 0.1795 0.2103 -0.0061 -0.0043 0.0278  138 HIS   A C   
2939 C  C   B HIS   A 138 ? 0.1405 0.1771 0.1890 -0.0071 0.0068  0.0212  138 HIS   A C   
2940 O  O   A HIS   A 138 ? 0.1429 0.1844 0.2098 -0.0086 -0.0035 0.0240  138 HIS   A O   
2941 O  O   B HIS   A 138 ? 0.1449 0.1810 0.1883 -0.0103 0.0054  0.0224  138 HIS   A O   
2942 C  CB  A HIS   A 138 ? 0.1665 0.2130 0.2112 -0.0148 -0.0219 0.0196  138 HIS   A CB  
2943 C  CB  B HIS   A 138 ? 0.1493 0.1847 0.1807 -0.0020 0.0180  -0.0152 138 HIS   A CB  
2944 C  CG  A HIS   A 138 ? 0.1859 0.2223 0.2166 -0.0214 -0.0180 0.0132  138 HIS   A CG  
2945 C  CG  B HIS   A 138 ? 0.1539 0.1812 0.1824 -0.0029 0.0137  -0.0291 138 HIS   A CG  
2946 N  ND1 A HIS   A 138 ? 0.2029 0.2321 0.2400 -0.0239 -0.0150 0.0051  138 HIS   A ND1 
2947 N  ND1 B HIS   A 138 ? 0.1605 0.1829 0.1984 0.0004  0.0073  -0.0331 138 HIS   A ND1 
2948 C  CD2 A HIS   A 138 ? 0.1907 0.2267 0.2195 -0.0140 -0.0108 0.0144  138 HIS   A CD2 
2949 C  CD2 B HIS   A 138 ? 0.1527 0.1757 0.1811 0.0009  0.0154  -0.0320 138 HIS   A CD2 
2950 C  CE1 A HIS   A 138 ? 0.2076 0.2360 0.2437 -0.0120 -0.0134 0.0083  138 HIS   A CE1 
2951 C  CE1 B HIS   A 138 ? 0.1602 0.1785 0.1989 0.0038  0.0034  -0.0334 138 HIS   A CE1 
2952 N  NE2 A HIS   A 138 ? 0.1990 0.2350 0.2272 -0.0072 -0.0043 0.0083  138 HIS   A NE2 
2953 N  NE2 B HIS   A 138 ? 0.1563 0.1755 0.1908 0.0035  0.0107  -0.0348 138 HIS   A NE2 
2968 N  N   . SER   A 139 ? 0.1304 0.1683 0.1961 -0.0060 -0.0058 0.0312  139 SER   A N   
2969 C  CA  . SER   A 139 ? 0.1292 0.1609 0.2025 -0.0084 0.0014  0.0314  139 SER   A CA  
2970 C  C   . SER   A 139 ? 0.1249 0.1522 0.2001 -0.0091 0.0044  0.0219  139 SER   A C   
2971 O  O   . SER   A 139 ? 0.1214 0.1502 0.2188 -0.0116 0.0017  0.0277  139 SER   A O   
2972 C  CB  . SER   A 139 ? 0.1287 0.1599 0.2075 -0.0145 -0.0038 0.0341  139 SER   A CB  
2973 O  OG  . SER   A 139 ? 0.1379 0.1571 0.2111 -0.0196 -0.0153 0.0403  139 SER   A OG  
2980 N  N   A LEU   A 140 ? 0.1204 0.1528 0.1991 -0.0100 -0.0079 0.0309  140 LEU   A N   
2981 N  N   B LEU   A 140 ? 0.1282 0.1434 0.1745 -0.0095 0.0089  0.0251  140 LEU   A N   
2982 C  CA  A LEU   A 140 ? 0.1236 0.1446 0.2026 -0.0097 -0.0035 0.0260  140 LEU   A CA  
2983 C  CA  B LEU   A 140 ? 0.1319 0.1307 0.1614 -0.0115 0.0143  0.0200  140 LEU   A CA  
2984 C  C   A LEU   A 140 ? 0.1143 0.1539 0.2043 -0.0110 0.0035  0.0255  140 LEU   A C   
2985 C  C   B LEU   A 140 ? 0.1384 0.1392 0.1673 -0.0093 0.0204  0.0188  140 LEU   A C   
2986 O  O   A LEU   A 140 ? 0.1191 0.1595 0.2118 -0.0017 0.0021  0.0307  140 LEU   A O   
2987 O  O   B LEU   A 140 ? 0.1394 0.1381 0.1738 -0.0038 0.0241  0.0167  140 LEU   A O   
2988 C  CB  A LEU   A 140 ? 0.1336 0.1499 0.2194 -0.0131 -0.0076 0.0177  140 LEU   A CB  
2989 C  CB  B LEU   A 140 ? 0.1235 0.1213 0.1503 -0.0153 0.0122  0.0231  140 LEU   A CB  
2990 C  CG  A LEU   A 140 ? 0.1317 0.1620 0.2284 -0.0096 0.0081  0.0241  140 LEU   A CG  
2991 C  CG  B LEU   A 140 ? 0.1180 0.1207 0.1490 -0.0125 0.0123  0.0323  140 LEU   A CG  
2992 C  CD1 A LEU   A 140 ? 0.1337 0.1679 0.2437 0.0030  -0.0029 0.0201  140 LEU   A CD1 
2993 C  CD1 B LEU   A 140 ? 0.1183 0.1278 0.1325 -0.0075 0.0174  0.0352  140 LEU   A CD1 
2994 C  CD2 A LEU   A 140 ? 0.1345 0.1650 0.2247 -0.0108 0.0099  0.0171  140 LEU   A CD2 
2995 C  CD2 B LEU   A 140 ? 0.1169 0.1215 0.1622 -0.0096 0.0090  0.0394  140 LEU   A CD2 
3018 N  N   A ARG   A 141 ? 0.1195 0.1537 0.2126 -0.0107 -0.0019 0.0168  141 ARG   A N   
3019 N  N   B ARG   A 141 ? 0.1502 0.1487 0.1756 -0.0062 0.0174  0.0172  141 ARG   A N   
3020 C  CA  A ARG   A 141 ? 0.1333 0.1634 0.2269 -0.0187 -0.0104 0.0003  141 ARG   A CA  
3021 C  CA  B ARG   A 141 ? 0.1619 0.1644 0.1858 -0.0082 0.0178  0.0070  141 ARG   A CA  
3022 C  C   A ARG   A 141 ? 0.1319 0.1496 0.2224 -0.0162 -0.0075 0.0019  141 ARG   A C   
3023 C  C   B ARG   A 141 ? 0.1572 0.1582 0.1853 -0.0110 0.0162  0.0107  141 ARG   A C   
3024 O  O   A ARG   A 141 ? 0.1290 0.1455 0.2339 -0.0106 0.0079  -0.0022 141 ARG   A O   
3025 O  O   B ARG   A 141 ? 0.1578 0.1595 0.1988 -0.0139 0.0169  0.0140  141 ARG   A O   
3026 C  CB  A ARG   A 141 ? 0.1394 0.1879 0.2384 -0.0187 -0.0039 -0.0223 141 ARG   A CB  
3027 C  CB  B ARG   A 141 ? 0.1787 0.1866 0.1981 -0.0032 0.0213  -0.0001 141 ARG   A CB  
3028 C  CG  A ARG   A 141 ? 0.1601 0.2130 0.2455 -0.0218 0.0204  -0.0310 141 ARG   A CG  
3029 C  CG  B ARG   A 141 ? 0.2002 0.2088 0.2166 0.0002  0.0284  -0.0020 141 ARG   A CG  
3030 C  CD  A ARG   A 141 ? 0.1860 0.2279 0.2644 -0.0412 0.0192  -0.0417 141 ARG   A CD  
3031 C  CD  B ARG   A 141 ? 0.2161 0.2267 0.2316 0.0053  0.0263  -0.0074 141 ARG   A CD  
3032 N  NE  A ARG   A 141 ? 0.1852 0.2522 0.2781 -0.0431 -0.0006 -0.0352 141 ARG   A NE  
3033 N  NE  B ARG   A 141 ? 0.2218 0.2322 0.2178 0.0081  0.0316  -0.0033 141 ARG   A NE  
3034 C  CZ  A ARG   A 141 ? 0.1890 0.2758 0.2841 -0.0557 0.0051  -0.0157 141 ARG   A CZ  
3035 C  CZ  B ARG   A 141 ? 0.2274 0.2321 0.2003 0.0118  0.0416  0.0116  141 ARG   A CZ  
3036 N  NH1 A ARG   A 141 ? 0.1763 0.2815 0.2773 -0.0708 0.0331  -0.0129 141 ARG   A NH1 
3037 N  NH1 B ARG   A 141 ? 0.2233 0.2291 0.1981 0.0101  0.0497  0.0222  141 ARG   A NH1 
3038 N  NH2 A ARG   A 141 ? 0.1973 0.2889 0.2956 -0.0465 -0.0112 -0.0056 141 ARG   A NH2 
3039 N  NH2 B ARG   A 141 ? 0.2382 0.2375 0.1996 0.0134  0.0400  0.0145  141 ARG   A NH2 
3066 N  N   A VAL   A 142 ? 0.1263 0.1445 0.2120 -0.0106 -0.0054 0.0014  142 VAL   A N   
3067 N  N   B VAL   A 142 ? 0.1479 0.1576 0.1784 -0.0103 0.0166  0.0111  142 VAL   A N   
3068 C  CA  A VAL   A 142 ? 0.1320 0.1477 0.2085 -0.0044 0.0146  0.0069  142 VAL   A CA  
3069 C  CA  B VAL   A 142 ? 0.1434 0.1561 0.1747 -0.0077 0.0138  0.0138  142 VAL   A CA  
3070 C  C   A VAL   A 142 ? 0.1226 0.1454 0.2017 -0.0116 0.0107  0.0096  142 VAL   A C   
3071 C  C   B VAL   A 142 ? 0.1329 0.1500 0.1825 -0.0109 0.0055  0.0134  142 VAL   A C   
3072 O  O   A VAL   A 142 ? 0.1266 0.1474 0.2055 0.0006  0.0117  0.0148  142 VAL   A O   
3073 O  O   B VAL   A 142 ? 0.1338 0.1506 0.1811 -0.0049 0.0018  0.0156  142 VAL   A O   
3074 C  CB  A VAL   A 142 ? 0.1418 0.1520 0.2092 -0.0043 0.0172  0.0128  142 VAL   A CB  
3075 C  CB  B VAL   A 142 ? 0.1459 0.1634 0.1693 -0.0046 0.0132  0.0157  142 VAL   A CB  
3076 C  CG1 A VAL   A 142 ? 0.1431 0.1426 0.2087 -0.0158 0.0221  0.0108  142 VAL   A CG1 
3077 C  CG1 B VAL   A 142 ? 0.1483 0.1661 0.1698 -0.0085 0.0115  0.0073  142 VAL   A CG1 
3078 C  CG2 A VAL   A 142 ? 0.1555 0.1645 0.2324 0.0008  0.0172  0.0096  142 VAL   A CG2 
3079 C  CG2 B VAL   A 142 ? 0.1539 0.1667 0.1760 0.0009  0.0099  0.0223  142 VAL   A CG2 
3098 N  N   . CYS   A 143 ? 0.1293 0.1474 0.1905 -0.0160 0.0031  0.0117  143 CYS   A N   
3099 C  CA  . CYS   A 143 ? 0.1290 0.1484 0.2045 -0.0112 0.0108  0.0178  143 CYS   A CA  
3100 C  C   . CYS   A 143 ? 0.1250 0.1459 0.2142 -0.0141 0.0052  0.0274  143 CYS   A C   
3101 O  O   . CYS   A 143 ? 0.1225 0.1477 0.2142 -0.0088 0.0048  0.0314  143 CYS   A O   
3102 C  CB  . CYS   A 143 ? 0.1329 0.1488 0.2013 -0.0070 0.0105  0.0258  143 CYS   A CB  
3103 S  SG  . CYS   A 143 ? 0.1512 0.1563 0.2031 0.0014  0.0102  0.0201  143 CYS   A SG  
3110 N  N   . VAL   A 144 ? 0.1251 0.1495 0.2336 -0.0109 0.0074  0.0317  144 VAL   A N   
3111 C  CA  . VAL   A 144 ? 0.1302 0.1602 0.2587 -0.0152 0.0172  0.0345  144 VAL   A CA  
3112 C  C   . VAL   A 144 ? 0.1336 0.1504 0.2448 -0.0186 0.0007  0.0318  144 VAL   A C   
3113 O  O   . VAL   A 144 ? 0.1508 0.1567 0.2508 -0.0110 -0.0087 0.0354  144 VAL   A O   
3114 C  CB  . VAL   A 144 ? 0.1542 0.1815 0.3131 -0.0020 0.0406  0.0361  144 VAL   A CB  
3115 C  CG1 . VAL   A 144 ? 0.1625 0.2052 0.3557 -0.0115 0.0286  0.0323  144 VAL   A CG1 
3116 C  CG2 . VAL   A 144 ? 0.1393 0.1881 0.3204 -0.0026 0.0464  0.0479  144 VAL   A CG2 
3126 N  N   . ASP   A 145 ? 0.1379 0.1448 0.2538 -0.0160 0.0058  0.0262  145 ASP   A N   
3127 C  CA  . ASP   A 145 ? 0.1494 0.1445 0.2562 -0.0178 0.0053  0.0147  145 ASP   A CA  
3128 C  C   . ASP   A 145 ? 0.1526 0.1409 0.2531 -0.0105 -0.0002 0.0097  145 ASP   A C   
3129 O  O   . ASP   A 145 ? 0.1660 0.1506 0.3111 -0.0109 -0.0040 -0.0260 145 ASP   A O   
3130 C  CB  . ASP   A 145 ? 0.1601 0.1779 0.2797 -0.0273 -0.0073 0.0083  145 ASP   A CB  
3131 C  CG  . ASP   A 145 ? 0.1761 0.2234 0.3074 -0.0457 -0.0232 0.0176  145 ASP   A CG  
3132 O  OD1 . ASP   A 145 ? 0.1668 0.2412 0.3132 -0.0585 -0.0091 0.0207  145 ASP   A OD1 
3133 O  OD2 . ASP   A 145 ? 0.1993 0.2467 0.3191 -0.0535 -0.0454 0.0184  145 ASP   A OD2 
3138 N  N   . THR   A 146 ? 0.1325 0.1364 0.2181 -0.0121 0.0073  0.0149  146 THR   A N   
3139 C  CA  . THR   A 146 ? 0.1313 0.1361 0.2125 -0.0087 0.0085  0.0098  146 THR   A CA  
3140 C  C   . THR   A 146 ? 0.1250 0.1317 0.2206 -0.0043 0.0115  0.0211  146 THR   A C   
3141 O  O   . THR   A 146 ? 0.1378 0.1447 0.2372 0.0016  -0.0033 0.0147  146 THR   A O   
3142 C  CB  . THR   A 146 ? 0.1314 0.1401 0.2175 -0.0004 0.0065  0.0172  146 THR   A CB  
3143 O  OG1 . THR   A 146 ? 0.1295 0.1554 0.2163 0.0021  0.0046  0.0126  146 THR   A OG1 
3144 C  CG2 . THR   A 146 ? 0.1287 0.1413 0.2383 -0.0054 0.0062  0.0195  146 THR   A CG2 
3152 N  N   . VAL   A 147 ? 0.1288 0.1392 0.2126 -0.0032 0.0127  0.0215  147 VAL   A N   
3153 C  CA  . VAL   A 147 ? 0.1287 0.1410 0.2170 -0.0059 0.0266  0.0312  147 VAL   A CA  
3154 C  C   . VAL   A 147 ? 0.1272 0.1357 0.2335 -0.0078 0.0233  0.0334  147 VAL   A C   
3155 O  O   . VAL   A 147 ? 0.1325 0.1416 0.2479 -0.0152 0.0128  0.0328  147 VAL   A O   
3156 C  CB  . VAL   A 147 ? 0.1394 0.1426 0.2095 -0.0140 0.0205  0.0292  147 VAL   A CB  
3157 C  CG1 . VAL   A 147 ? 0.1697 0.1454 0.2228 -0.0090 0.0176  0.0382  147 VAL   A CG1 
3158 C  CG2 . VAL   A 147 ? 0.1452 0.1392 0.2055 -0.0082 0.0128  0.0221  147 VAL   A CG2 
3168 N  N   . ARG   A 148 ? 0.1277 0.1368 0.2426 -0.0099 0.0231  0.0469  148 ARG   A N   
3169 C  CA  . ARG   A 148 ? 0.1375 0.1441 0.2450 -0.0148 0.0152  0.0538  148 ARG   A CA  
3170 C  C   . ARG   A 148 ? 0.1478 0.1457 0.2355 -0.0155 0.0145  0.0699  148 ARG   A C   
3171 O  O   . ARG   A 148 ? 0.1762 0.1591 0.2517 -0.0227 0.0195  0.0595  148 ARG   A O   
3172 C  CB  . ARG   A 148 ? 0.1437 0.1438 0.2547 -0.0065 0.0226  0.0493  148 ARG   A CB  
3173 C  CG  . ARG   A 148 ? 0.1628 0.1429 0.2892 -0.0084 0.0376  0.0350  148 ARG   A CG  
3174 C  CD  . ARG   A 148 ? 0.1776 0.1398 0.3077 -0.0089 0.0479  0.0528  148 ARG   A CD  
3175 N  NE  . ARG   A 148 ? 0.1709 0.1449 0.3031 0.0111  0.0544  0.0521  148 ARG   A NE  
3176 C  CZ  . ARG   A 148 ? 0.1650 0.1361 0.2866 0.0019  0.0430  0.0400  148 ARG   A CZ  
3177 N  NH1 . ARG   A 148 ? 0.1705 0.1408 0.2958 -0.0147 0.0392  0.0124  148 ARG   A NH1 
3178 N  NH2 . ARG   A 148 ? 0.1585 0.1562 0.2863 0.0121  0.0475  0.0469  148 ARG   A NH2 
3192 N  N   . THR   A 149 ? 0.1467 0.1559 0.2260 -0.0134 0.0036  0.0548  149 THR   A N   
3193 C  CA  . THR   A 149 ? 0.1441 0.1603 0.2284 -0.0101 0.0039  0.0561  149 THR   A CA  
3194 C  C   . THR   A 149 ? 0.1421 0.1553 0.2170 -0.0168 0.0042  0.0598  149 THR   A C   
3195 O  O   . THR   A 149 ? 0.1427 0.1662 0.2315 -0.0203 0.0091  0.0530  149 THR   A O   
3196 C  CB  . THR   A 149 ? 0.1454 0.1723 0.2404 -0.0160 0.0089  0.0560  149 THR   A CB  
3197 O  OG1 . THR   A 149 ? 0.1456 0.1584 0.2519 -0.0235 0.0049  0.0427  149 THR   A OG1 
3198 C  CG2 . THR   A 149 ? 0.1460 0.1888 0.2515 -0.0038 -0.0076 0.0462  149 THR   A CG2 
3206 N  N   . ASN   A 150 ? 0.1444 0.1637 0.2142 -0.0098 -0.0009 0.0639  150 ASN   A N   
3207 C  CA  . ASN   A 150 ? 0.1582 0.1726 0.2120 -0.0141 0.0045  0.0594  150 ASN   A CA  
3208 C  C   . ASN   A 150 ? 0.1395 0.1627 0.2037 -0.0163 0.0000  0.0526  150 ASN   A C   
3209 O  O   . ASN   A 150 ? 0.1513 0.1753 0.2319 -0.0193 -0.0160 0.0460  150 ASN   A O   
3210 C  CB  . ASN   A 150 ? 0.2039 0.2018 0.2407 -0.0194 0.0285  0.0778  150 ASN   A CB  
3211 C  CG  . ASN   A 150 ? 0.2569 0.2357 0.3031 -0.0213 0.0184  0.0801  150 ASN   A CG  
3212 O  OD1 . ASN   A 150 ? 0.2767 0.2437 0.3205 -0.0256 0.0252  0.0922  150 ASN   A OD1 
3213 N  ND2 . ASN   A 150 ? 0.2849 0.2583 0.3445 -0.0169 0.0057  0.0744  150 ASN   A ND2 
3220 N  N   . VAL   A 151 ? 0.1395 0.1479 0.2036 -0.0186 0.0013  0.0472  151 VAL   A N   
3221 C  CA  . VAL   A 151 ? 0.1474 0.1516 0.1963 -0.0229 -0.0004 0.0440  151 VAL   A CA  
3222 C  C   . VAL   A 151 ? 0.1356 0.1464 0.2061 -0.0261 0.0077  0.0492  151 VAL   A C   
3223 O  O   . VAL   A 151 ? 0.1483 0.1554 0.2351 -0.0201 0.0064  0.0412  151 VAL   A O   
3224 C  CB  . VAL   A 151 ? 0.1824 0.1677 0.1898 -0.0092 0.0012  0.0402  151 VAL   A CB  
3225 C  CG1 . VAL   A 151 ? 0.1809 0.1885 0.2161 -0.0152 -0.0050 0.0367  151 VAL   A CG1 
3226 C  CG2 . VAL   A 151 ? 0.1938 0.1605 0.1907 0.0003  0.0206  0.0380  151 VAL   A CG2 
3236 N  N   . TYR   A 152 ? 0.1382 0.1479 0.2042 -0.0226 0.0068  0.0462  152 TYR   A N   
3237 C  CA  . TYR   A 152 ? 0.1389 0.1550 0.1846 -0.0262 0.0027  0.0471  152 TYR   A CA  
3238 C  C   . TYR   A 152 ? 0.1383 0.1449 0.1749 -0.0217 0.0090  0.0442  152 TYR   A C   
3239 O  O   . TYR   A 152 ? 0.1442 0.1454 0.1845 -0.0252 0.0134  0.0347  152 TYR   A O   
3240 C  CB  . TYR   A 152 ? 0.1586 0.1686 0.1836 -0.0207 0.0161  0.0537  152 TYR   A CB  
3241 C  CG  . TYR   A 152 ? 0.1661 0.1916 0.1802 -0.0269 0.0187  0.0536  152 TYR   A CG  
3242 C  CD1 . TYR   A 152 ? 0.1807 0.2131 0.2021 -0.0096 0.0265  0.0539  152 TYR   A CD1 
3243 C  CD2 . TYR   A 152 ? 0.1740 0.2023 0.1707 -0.0373 0.0127  0.0472  152 TYR   A CD2 
3244 C  CE1 . TYR   A 152 ? 0.2192 0.2283 0.2075 -0.0060 0.0169  0.0628  152 TYR   A CE1 
3245 C  CE2 . TYR   A 152 ? 0.2080 0.2198 0.1928 -0.0362 0.0139  0.0534  152 TYR   A CE2 
3246 C  CZ  . TYR   A 152 ? 0.2364 0.2227 0.1996 -0.0236 0.0087  0.0788  152 TYR   A CZ  
3247 O  OH  . TYR   A 152 ? 0.2672 0.2409 0.2427 -0.0208 0.0093  0.0940  152 TYR   A OH  
3257 N  N   . LEU   A 153 ? 0.1344 0.1466 0.1866 -0.0224 0.0154  0.0436  153 LEU   A N   
3258 C  CA  . LEU   A 153 ? 0.1259 0.1471 0.1955 -0.0147 0.0097  0.0397  153 LEU   A CA  
3259 C  C   . LEU   A 153 ? 0.1337 0.1493 0.1971 -0.0083 0.0175  0.0401  153 LEU   A C   
3260 O  O   . LEU   A 153 ? 0.1374 0.1603 0.2281 -0.0122 0.0356  0.0405  153 LEU   A O   
3261 C  CB  . LEU   A 153 ? 0.1210 0.1491 0.2020 -0.0138 0.0161  0.0382  153 LEU   A CB  
3262 C  CG  . LEU   A 153 ? 0.1307 0.1495 0.1982 -0.0122 0.0087  0.0327  153 LEU   A CG  
3263 C  CD1 . LEU   A 153 ? 0.1477 0.1556 0.2004 -0.0098 0.0026  0.0305  153 LEU   A CD1 
3264 C  CD2 . LEU   A 153 ? 0.1373 0.1531 0.2026 -0.0169 0.0221  0.0120  153 LEU   A CD2 
3276 N  N   A ALA   A 154 ? 0.1318 0.1394 0.2004 -0.0099 0.0237  0.0378  154 ALA   A N   
3277 N  N   B ALA   A 154 ? 0.1372 0.1501 0.1759 -0.0013 0.0117  0.0342  154 ALA   A N   
3278 C  CA  A ALA   A 154 ? 0.1420 0.1399 0.1996 -0.0059 0.0279  0.0343  154 ALA   A CA  
3279 C  CA  B ALA   A 154 ? 0.1469 0.1537 0.1638 0.0061  0.0040  0.0269  154 ALA   A CA  
3280 C  C   A ALA   A 154 ? 0.1324 0.1324 0.1987 0.0000  0.0267  0.0359  154 ALA   A C   
3281 C  C   B ALA   A 154 ? 0.1449 0.1566 0.1543 0.0039  0.0027  0.0239  154 ALA   A C   
3282 O  O   A ALA   A 154 ? 0.1412 0.1449 0.2117 -0.0058 0.0298  0.0332  154 ALA   A O   
3283 O  O   B ALA   A 154 ? 0.1501 0.1591 0.1496 -0.0008 0.0028  0.0197  154 ALA   A O   
3284 C  CB  A ALA   A 154 ? 0.1482 0.1457 0.2119 -0.0013 0.0166  0.0323  154 ALA   A CB  
3285 C  CB  B ALA   A 154 ? 0.1499 0.1524 0.1697 0.0164  -0.0072 0.0244  154 ALA   A CB  
3296 N  N   A VAL   A 155 ? 0.1192 0.1109 0.1645 0.0094  0.0246  0.0572  155 VAL   A N   
3297 N  N   B VAL   A 155 ? 0.1397 0.1537 0.1479 0.0057  0.0061  0.0320  155 VAL   A N   
3298 C  CA  A VAL   A 155 ? 0.1395 0.1315 0.1976 0.0076  0.0220  0.0519  155 VAL   A CA  
3299 C  CA  B VAL   A 155 ? 0.1543 0.1667 0.1615 0.0013  0.0097  0.0324  155 VAL   A CA  
3300 C  CA  T VAL   A 155 ? 0.1755 0.1673 0.1955 -0.0074 0.0273  0.0407  155 VAL   A CA  
3301 C  C   A VAL   A 155 ? 0.1465 0.1438 0.2282 0.0200  0.0196  0.0493  155 VAL   A C   
3302 C  C   B VAL   A 155 ? 0.1681 0.1767 0.1886 0.0101  0.0004  0.0343  155 VAL   A C   
3303 C  C   T VAL   A 155 ? 0.1740 0.1657 0.1941 0.0010  0.0318  0.0471  155 VAL   A C   
3304 O  O   A VAL   A 155 ? 0.1402 0.1428 0.2348 0.0223  0.0268  0.0345  155 VAL   A O   
3305 O  O   B VAL   A 155 ? 0.1666 0.1801 0.1745 0.0173  -0.0056 0.0274  155 VAL   A O   
3306 O  O   T VAL   A 155 ? 0.1691 0.1695 0.1820 0.0012  0.0309  0.0403  155 VAL   A O   
3307 C  CB  A VAL   A 155 ? 0.1461 0.1429 0.1873 0.0129  0.0188  0.0449  155 VAL   A CB  
3308 C  CB  B VAL   A 155 ? 0.1544 0.1705 0.1583 0.0020  0.0100  0.0208  155 VAL   A CB  
3309 C  CB  T VAL   A 155 ? 0.1760 0.1715 0.1899 -0.0052 0.0189  0.0358  155 VAL   A CB  
3310 C  CG1 A VAL   A 155 ? 0.1553 0.1564 0.1851 0.0140  0.0181  0.0469  155 VAL   A CG1 
3311 C  CG1 B VAL   A 155 ? 0.1590 0.1785 0.1579 0.0063  0.0110  0.0184  155 VAL   A CG1 
3312 C  CG1 T VAL   A 155 ? 0.1810 0.1790 0.1893 -0.0022 0.0165  0.0345  155 VAL   A CG1 
3313 C  CG2 A VAL   A 155 ? 0.1583 0.1531 0.2007 0.0209  0.0030  0.0344  155 VAL   A CG2 
3314 C  CG2 B VAL   A 155 ? 0.1574 0.1721 0.1601 0.0060  0.0067  0.0177  155 VAL   A CG2 
3315 C  CG2 T VAL   A 155 ? 0.1804 0.1752 0.1967 -0.0017 0.0086  0.0305  155 VAL   A CG2 
3341 N  N   A PHE   A 156 ? 0.1625 0.1606 0.2564 0.0233  0.0233  0.0646  156 PHE   A N   
3342 N  N   B PHE   A 156 ? 0.1858 0.1830 0.2188 0.0062  0.0010  0.0468  156 PHE   A N   
3343 N  N   T PHE   A 156 ? 0.1824 0.1609 0.2069 0.0042  0.0447  0.0623  156 PHE   A N   
3344 C  CA  A PHE   A 156 ? 0.1821 0.1765 0.2790 0.0315  0.0206  0.0679  156 PHE   A CA  
3345 C  CA  B PHE   A 156 ? 0.2051 0.1890 0.2440 0.0033  -0.0022 0.0507  156 PHE   A CA  
3346 C  CA  T PHE   A 156 ? 0.1970 0.1612 0.2134 0.0118  0.0508  0.0650  156 PHE   A CA  
3347 C  C   A PHE   A 156 ? 0.1742 0.1811 0.2840 0.0405  0.0394  0.0711  156 PHE   A C   
3348 C  C   B PHE   A 156 ? 0.2169 0.2047 0.2621 0.0112  0.0066  0.0530  156 PHE   A C   
3349 C  C   T PHE   A 156 ? 0.1939 0.1721 0.2182 0.0193  0.0710  0.0724  156 PHE   A C   
3350 O  O   A PHE   A 156 ? 0.1776 0.1844 0.3018 0.0302  0.0522  0.0609  156 PHE   A O   
3351 O  O   B PHE   A 156 ? 0.2201 0.2050 0.2661 0.0107  0.0101  0.0508  156 PHE   A O   
3352 O  O   T PHE   A 156 ? 0.2002 0.1769 0.2210 0.0190  0.0938  0.0626  156 PHE   A O   
3353 C  CB  A PHE   A 156 ? 0.2043 0.1899 0.2871 0.0297  0.0056  0.0688  156 PHE   A CB  
3354 C  CB  B PHE   A 156 ? 0.2058 0.1807 0.2409 -0.0091 -0.0096 0.0537  156 PHE   A CB  
3355 C  CB  T PHE   A 156 ? 0.2039 0.1488 0.2011 0.0132  0.0442  0.0649  156 PHE   A CB  
3356 C  CG  A PHE   A 156 ? 0.2267 0.2010 0.2975 0.0352  -0.0050 0.0581  156 PHE   A CG  
3357 C  CG  B PHE   A 156 ? 0.2067 0.1782 0.2400 -0.0163 -0.0152 0.0563  156 PHE   A CG  
3358 C  CG  T PHE   A 156 ? 0.2109 0.1491 0.1884 0.0167  0.0394  0.0600  156 PHE   A CG  
3359 C  CD1 A PHE   A 156 ? 0.2360 0.2035 0.3027 0.0408  0.0011  0.0479  156 PHE   A CD1 
3360 C  CD1 B PHE   A 156 ? 0.2018 0.1765 0.2489 -0.0231 -0.0096 0.0528  156 PHE   A CD1 
3361 C  CD1 T PHE   A 156 ? 0.2157 0.1537 0.2128 0.0223  0.0280  0.0421  156 PHE   A CD1 
3362 C  CD2 A PHE   A 156 ? 0.2373 0.2121 0.3070 0.0433  -0.0142 0.0521  156 PHE   A CD2 
3363 C  CD2 B PHE   A 156 ? 0.2110 0.1847 0.2585 -0.0142 -0.0196 0.0524  156 PHE   A CD2 
3364 C  CD2 T PHE   A 156 ? 0.2131 0.1483 0.1844 0.0207  0.0471  0.0575  156 PHE   A CD2 
3365 C  CE1 A PHE   A 156 ? 0.2448 0.2083 0.3119 0.0440  0.0022  0.0386  156 PHE   A CE1 
3366 C  CE1 B PHE   A 156 ? 0.2020 0.1792 0.2578 -0.0255 -0.0069 0.0446  156 PHE   A CE1 
3367 C  CE1 T PHE   A 156 ? 0.2202 0.1549 0.2255 0.0226  0.0249  0.0311  156 PHE   A CE1 
3368 C  CE2 A PHE   A 156 ? 0.2502 0.2197 0.3169 0.0463  -0.0119 0.0365  156 PHE   A CE2 
3369 C  CE2 B PHE   A 156 ? 0.2151 0.1878 0.2711 -0.0179 -0.0201 0.0444  156 PHE   A CE2 
3370 C  CE2 T PHE   A 156 ? 0.2202 0.1538 0.1987 0.0208  0.0415  0.0440  156 PHE   A CE2 
3371 C  CZ  A PHE   A 156 ? 0.2508 0.2180 0.3170 0.0463  -0.0003 0.0319  156 PHE   A CZ  
3372 C  CZ  B PHE   A 156 ? 0.2071 0.1811 0.2684 -0.0264 -0.0111 0.0439  156 PHE   A CZ  
3373 C  CZ  T PHE   A 156 ? 0.2204 0.1513 0.2223 0.0176  0.0318  0.0322  156 PHE   A CZ  
3401 N  N   A ASP   A 157 ? 0.1671 0.1929 0.2798 0.0483  0.0346  0.0894  157 ASP   A N   
3402 N  N   B ASP   A 157 ? 0.2232 0.2222 0.2736 0.0166  0.0031  0.0572  157 ASP   A N   
3403 N  N   T ASP   A 157 ? 0.1796 0.1862 0.2238 0.0232  0.0595  0.0940  157 ASP   A N   
3404 C  CA  A ASP   A 157 ? 0.1743 0.2153 0.2849 0.0480  0.0345  0.0926  157 ASP   A CA  
3405 C  CA  B ASP   A 157 ? 0.2343 0.2463 0.2897 0.0163  0.0010  0.0607  157 ASP   A CA  
3406 C  CA  T ASP   A 157 ? 0.1740 0.2031 0.2352 0.0314  0.0486  0.0968  157 ASP   A CA  
3407 C  C   A ASP   A 157 ? 0.1590 0.2281 0.2928 0.0490  0.0380  0.1025  157 ASP   A C   
3408 C  C   B ASP   A 157 ? 0.2246 0.2535 0.2987 0.0216  0.0017  0.0630  157 ASP   A C   
3409 C  C   T ASP   A 157 ? 0.1768 0.2213 0.2470 0.0331  0.0538  0.1015  157 ASP   A C   
3410 O  O   A ASP   A 157 ? 0.1487 0.2202 0.2686 0.0486  0.0227  0.1212  157 ASP   A O   
3411 O  O   B ASP   A 157 ? 0.2313 0.2578 0.2997 0.0211  0.0048  0.0638  157 ASP   A O   
3412 O  O   T ASP   A 157 ? 0.1674 0.2188 0.2367 0.0319  0.0568  0.1047  157 ASP   A O   
3413 C  CB  A ASP   A 157 ? 0.1915 0.2238 0.2872 0.0549  0.0336  0.0834  157 ASP   A CB  
3414 C  CB  B ASP   A 157 ? 0.2517 0.2620 0.3007 0.0116  -0.0030 0.0589  157 ASP   A CB  
3415 C  CB  T ASP   A 157 ? 0.1673 0.2016 0.2399 0.0429  0.0360  0.0894  157 ASP   A CB  
3416 C  CG  A ASP   A 157 ? 0.2112 0.2307 0.2993 0.0620  0.0265  0.0788  157 ASP   A CG  
3417 C  CG  B ASP   A 157 ? 0.2692 0.2769 0.3134 0.0075  -0.0084 0.0581  157 ASP   A CG  
3418 C  CG  T ASP   A 157 ? 0.1592 0.1977 0.2434 0.0541  0.0286  0.0814  157 ASP   A CG  
3419 O  OD1 A ASP   A 157 ? 0.2326 0.2354 0.3216 0.0573  0.0125  0.0727  157 ASP   A OD1 
3420 O  OD1 B ASP   A 157 ? 0.2775 0.2794 0.3149 0.0028  -0.0092 0.0668  157 ASP   A OD1 
3421 O  OD1 T ASP   A 157 ? 0.1485 0.1873 0.2544 0.0613  0.0392  0.0644  157 ASP   A OD1 
3422 O  OD2 A ASP   A 157 ? 0.1990 0.2262 0.2991 0.0650  0.0356  0.0893  157 ASP   A OD2 
3423 O  OD2 B ASP   A 157 ? 0.2750 0.2824 0.3282 0.0096  -0.0150 0.0508  157 ASP   A OD2 
3424 O  OD2 T ASP   A 157 ? 0.1526 0.1964 0.2332 0.0605  0.0172  0.0884  157 ASP   A OD2 
3437 N  N   A LYS   A 158 ? 0.1689 0.2481 0.3170 0.0446  0.0547  0.0921  158 LYS   A N   
3438 N  N   B LYS   A 158 ? 0.2129 0.2542 0.3034 0.0243  -0.0018 0.0642  158 LYS   A N   
3439 N  N   T LYS   A 158 ? 0.1959 0.2424 0.2718 0.0328  0.0556  0.0899  158 LYS   A N   
3440 C  CA  A LYS   A 158 ? 0.1719 0.2643 0.3340 0.0531  0.0613  0.0848  158 LYS   A CA  
3441 C  CA  B LYS   A 158 ? 0.2085 0.2566 0.3048 0.0241  0.0080  0.0616  158 LYS   A CA  
3442 C  CA  T LYS   A 158 ? 0.2090 0.2610 0.2963 0.0386  0.0521  0.0767  158 LYS   A CA  
3443 C  C   A LYS   A 158 ? 0.1622 0.2717 0.3283 0.0616  0.0476  0.0889  158 LYS   A C   
3444 C  C   B LYS   A 158 ? 0.1845 0.2507 0.2859 0.0207  -0.0051 0.0633  158 LYS   A C   
3445 C  C   T LYS   A 158 ? 0.2080 0.2656 0.2958 0.0440  0.0397  0.0728  158 LYS   A C   
3446 O  O   A LYS   A 158 ? 0.1608 0.2770 0.3354 0.0547  0.0483  0.0906  158 LYS   A O   
3447 O  O   B LYS   A 158 ? 0.1762 0.2520 0.2846 0.0095  -0.0013 0.0662  158 LYS   A O   
3448 O  O   T LYS   A 158 ? 0.2063 0.2672 0.3011 0.0443  0.0377  0.0731  158 LYS   A O   
3449 C  CB  A LYS   A 158 ? 0.1919 0.2731 0.3611 0.0507  0.0818  0.0761  158 LYS   A CB  
3450 C  CB  B LYS   A 158 ? 0.2259 0.2684 0.3245 0.0234  0.0275  0.0596  158 LYS   A CB  
3451 C  CB  T LYS   A 158 ? 0.2283 0.2743 0.3309 0.0375  0.0612  0.0634  158 LYS   A CB  
3452 C  CG  A LYS   A 158 ? 0.2147 0.2815 0.3893 0.0477  0.0898  0.0765  158 LYS   A CG  
3453 C  CG  B LYS   A 158 ? 0.2428 0.2797 0.3470 0.0230  0.0450  0.0636  158 LYS   A CG  
3454 C  CG  T LYS   A 158 ? 0.2463 0.2855 0.3621 0.0369  0.0651  0.0591  158 LYS   A CG  
3455 C  CD  A LYS   A 158 ? 0.2313 0.2897 0.4119 0.0471  0.1004  0.0811  158 LYS   A CD  
3456 C  CD  B LYS   A 158 ? 0.2564 0.2897 0.3660 0.0210  0.0637  0.0705  158 LYS   A CD  
3457 C  CD  T LYS   A 158 ? 0.2614 0.2955 0.3924 0.0392  0.0669  0.0595  158 LYS   A CD  
3458 C  CE  A LYS   A 158 ? 0.2421 0.2939 0.4201 0.0427  0.1119  0.0918  158 LYS   A CE  
3459 C  CE  B LYS   A 158 ? 0.2625 0.2948 0.3754 0.0229  0.0792  0.0809  158 LYS   A CE  
3460 C  CE  T LYS   A 158 ? 0.2727 0.3016 0.4109 0.0396  0.0683  0.0636  158 LYS   A CE  
3461 N  NZ  A LYS   A 158 ? 0.2460 0.2955 0.4254 0.0376  0.1192  0.0976  158 LYS   A NZ  
3462 N  NZ  B LYS   A 158 ? 0.2649 0.2975 0.3844 0.0225  0.0866  0.0870  158 LYS   A NZ  
3463 N  NZ  T LYS   A 158 ? 0.2795 0.3048 0.4215 0.0404  0.0685  0.0661  158 LYS   A NZ  
3503 N  N   A ASN   A 159 ? 0.1623 0.2730 0.3260 0.0633  0.0332  0.0881  159 ASN   A N   
3504 N  N   B ASN   A 159 ? 0.1788 0.2488 0.2777 0.0283  -0.0165 0.0597  159 ASN   A N   
3505 N  N   T ASN   A 159 ? 0.2123 0.2668 0.3001 0.0406  0.0320  0.0664  159 ASN   A N   
3506 C  CA  A ASN   A 159 ? 0.1743 0.2741 0.3125 0.0588  0.0113  0.0926  159 ASN   A CA  
3507 C  CA  B ASN   A 159 ? 0.1727 0.2488 0.2702 0.0342  -0.0150 0.0600  159 ASN   A CA  
3508 C  CA  T ASN   A 159 ? 0.2241 0.2679 0.2976 0.0336  0.0201  0.0630  159 ASN   A CA  
3509 C  C   A ASN   A 159 ? 0.1653 0.2765 0.2929 0.0511  0.0107  0.0942  159 ASN   A C   
3510 C  C   B ASN   A 159 ? 0.1523 0.2489 0.2627 0.0410  -0.0174 0.0725  159 ASN   A C   
3511 C  C   T ASN   A 159 ? 0.2283 0.2716 0.2922 0.0277  0.0214  0.0565  159 ASN   A C   
3512 O  O   A ASN   A 159 ? 0.1588 0.2704 0.3004 0.0609  -0.0000 0.0809  159 ASN   A O   
3513 O  O   B ASN   A 159 ? 0.1353 0.2542 0.2680 0.0512  -0.0288 0.0873  159 ASN   A O   
3514 O  O   T ASN   A 159 ? 0.2272 0.2666 0.2939 0.0325  0.0161  0.0475  159 ASN   A O   
3515 C  CB  A ASN   A 159 ? 0.1906 0.2747 0.3275 0.0582  0.0038  0.0914  159 ASN   A CB  
3516 C  CB  B ASN   A 159 ? 0.1863 0.2502 0.2774 0.0306  -0.0027 0.0459  159 ASN   A CB  
3517 C  CB  T ASN   A 159 ? 0.2306 0.2669 0.3093 0.0318  0.0116  0.0653  159 ASN   A CB  
3518 C  CG  A ASN   A 159 ? 0.2078 0.2800 0.3480 0.0515  0.0016  0.0779  159 ASN   A CG  
3519 C  CG  B ASN   A 159 ? 0.1975 0.2558 0.2851 0.0196  0.0059  0.0296  159 ASN   A CG  
3520 C  CG  T ASN   A 159 ? 0.2378 0.2682 0.3239 0.0284  0.0069  0.0597  159 ASN   A CG  
3521 O  OD1 A ASN   A 159 ? 0.2160 0.2892 0.3640 0.0441  0.0116  0.0634  159 ASN   A OD1 
3522 O  OD1 B ASN   A 159 ? 0.2087 0.2615 0.2974 0.0158  0.0112  0.0133  159 ASN   A OD1 
3523 O  OD1 T ASN   A 159 ? 0.2407 0.2739 0.3378 0.0248  0.0139  0.0485  159 ASN   A OD1 
3524 N  ND2 A ASN   A 159 ? 0.2137 0.2809 0.3573 0.0518  -0.0058 0.0738  159 ASN   A ND2 
3525 N  ND2 B ASN   A 159 ? 0.1965 0.2609 0.2817 0.0130  0.0038  0.0329  159 ASN   A ND2 
3526 N  ND2 T ASN   A 159 ? 0.2408 0.2687 0.3288 0.0286  -0.0007 0.0599  159 ASN   A ND2 
3545 N  N   A LEU   A 160 ? 0.1536 0.2773 0.2622 0.0370  0.0082  0.1105  160 LEU   A N   
3546 N  N   B LEU   A 160 ? 0.1512 0.2474 0.2564 0.0319  -0.0176 0.0752  160 LEU   A N   
3547 N  N   T LEU   A 160 ? 0.2299 0.2755 0.2836 0.0171  0.0206  0.0597  160 LEU   A N   
3548 C  CA  A LEU   A 160 ? 0.1483 0.2725 0.2213 0.0184  0.0133  0.1280  160 LEU   A CA  
3549 C  CA  B LEU   A 160 ? 0.1524 0.2454 0.2374 0.0303  -0.0009 0.0786  160 LEU   A CA  
3550 C  CA  T LEU   A 160 ? 0.2334 0.2759 0.2659 0.0054  0.0210  0.0650  160 LEU   A CA  
3551 C  C   A LEU   A 160 ? 0.1233 0.2676 0.1932 0.0107  0.0180  0.1304  160 LEU   A C   
3552 C  C   B LEU   A 160 ? 0.1427 0.2441 0.2054 0.0297  0.0152  0.0740  160 LEU   A C   
3553 O  O   A LEU   A 160 ? 0.1112 0.2720 0.1784 0.0087  0.0048  0.1260  160 LEU   A O   
3554 O  O   B LEU   A 160 ? 0.1373 0.2459 0.1969 0.0268  0.0196  0.0824  160 LEU   A O   
3555 C  CB  A LEU   A 160 ? 0.1557 0.2768 0.2039 0.0082  0.0181  0.1258  160 LEU   A CB  
3556 C  CB  B LEU   A 160 ? 0.1647 0.2484 0.2447 0.0226  0.0128  0.0719  160 LEU   A CB  
3557 C  CB  T LEU   A 160 ? 0.2330 0.2766 0.2475 -0.0062 0.0242  0.0635  160 LEU   A CB  
3558 C  CG  A LEU   A 160 ? 0.1647 0.2830 0.2224 -0.0027 0.0078  0.0965  160 LEU   A CG  
3559 C  CG  B LEU   A 160 ? 0.1727 0.2530 0.2560 0.0161  0.0228  0.0551  160 LEU   A CG  
3560 C  CG  T LEU   A 160 ? 0.2332 0.2784 0.2437 -0.0168 0.0217  0.0507  160 LEU   A CG  
3561 C  CD1 A LEU   A 160 ? 0.1702 0.2896 0.2353 -0.0107 0.0085  0.0867  160 LEU   A CD1 
3562 C  CD1 B LEU   A 160 ? 0.1781 0.2559 0.2623 0.0097  0.0234  0.0491  160 LEU   A CD1 
3563 C  CD1 T LEU   A 160 ? 0.2347 0.2823 0.2461 -0.0210 0.0214  0.0457  160 LEU   A CD1 
3564 C  CD2 A LEU   A 160 ? 0.1651 0.2809 0.2282 -0.0042 0.0106  0.0815  160 LEU   A CD2 
3565 C  CD2 B LEU   A 160 ? 0.1728 0.2535 0.2548 0.0168  0.0342  0.0476  160 LEU   A CD2 
3566 C  CD2 T LEU   A 160 ? 0.2321 0.2757 0.2401 -0.0201 0.0238  0.0435  160 LEU   A CD2 
3599 N  N   A TYR   A 161 ? 0.1324 0.2624 0.2288 0.0072  0.0266  0.1131  161 TYR   A N   
3600 N  N   B TYR   A 161 ? 0.1518 0.2431 0.2130 0.0316  0.0174  0.0551  161 TYR   A N   
3601 C  CA  A TYR   A 161 ? 0.1356 0.2516 0.2227 -0.0000 0.0217  0.1028  161 TYR   A CA  
3602 C  CA  B TYR   A 161 ? 0.1583 0.2372 0.1970 0.0314  0.0248  0.0393  161 TYR   A CA  
3603 C  C   A TYR   A 161 ? 0.1339 0.2746 0.2211 -0.0012 0.0153  0.0971  161 TYR   A C   
3604 C  C   B TYR   A 161 ? 0.1617 0.2479 0.1952 0.0296  0.0281  0.0384  161 TYR   A C   
3605 O  O   A TYR   A 161 ? 0.1284 0.2759 0.1964 -0.0084 0.0102  0.0942  161 TYR   A O   
3606 O  O   B TYR   A 161 ? 0.1578 0.2488 0.1793 0.0262  0.0380  0.0329  161 TYR   A O   
3607 C  CB  A TYR   A 161 ? 0.1480 0.2274 0.2240 -0.0051 0.0230  0.0832  161 TYR   A CB  
3608 C  CB  B TYR   A 161 ? 0.1682 0.2253 0.2013 0.0281  0.0244  0.0229  161 TYR   A CB  
3609 C  CG  A TYR   A 161 ? 0.1432 0.2055 0.2109 -0.0009 0.0177  0.0511  161 TYR   A CG  
3610 C  CG  B TYR   A 161 ? 0.1705 0.2120 0.1959 0.0296  0.0215  0.0081  161 TYR   A CG  
3611 C  CD1 A TYR   A 161 ? 0.1415 0.1959 0.2132 0.0022  0.0151  0.0327  161 TYR   A CD1 
3612 C  CD1 B TYR   A 161 ? 0.1731 0.2069 0.1920 0.0253  0.0195  0.0007  161 TYR   A CD1 
3613 C  CD2 A TYR   A 161 ? 0.1464 0.2035 0.2116 0.0063  0.0093  0.0360  161 TYR   A CD2 
3614 C  CD2 B TYR   A 161 ? 0.1715 0.2073 0.1900 0.0339  0.0193  0.0051  161 TYR   A CD2 
3615 C  CE1 A TYR   A 161 ? 0.1423 0.1868 0.1997 0.0063  0.0048  0.0285  161 TYR   A CE1 
3616 C  CE1 B TYR   A 161 ? 0.1776 0.2063 0.1953 0.0277  0.0179  0.0010  161 TYR   A CE1 
3617 C  CE2 A TYR   A 161 ? 0.1466 0.1922 0.1973 0.0012  0.0065  0.0373  161 TYR   A CE2 
3618 C  CE2 B TYR   A 161 ? 0.1770 0.2063 0.1939 0.0287  0.0197  0.0062  161 TYR   A CE2 
3619 C  CZ  A TYR   A 161 ? 0.1542 0.1844 0.2016 -0.0025 0.0006  0.0347  161 TYR   A CZ  
3620 C  CZ  B TYR   A 161 ? 0.1857 0.2087 0.2039 0.0263  0.0176  0.0044  161 TYR   A CZ  
3621 O  OH  A TYR   A 161 ? 0.1687 0.1737 0.2055 -0.0086 -0.0007 0.0465  161 TYR   A OH  
3622 O  OH  B TYR   A 161 ? 0.1999 0.2118 0.2234 0.0245  0.0085  0.0075  161 TYR   A OH  
3641 N  N   A ASP   A 162 ? 0.1308 0.2930 0.2430 0.0015  0.0242  0.0987  162 ASP   A N   
3642 N  N   B ASP   A 162 ? 0.1696 0.2586 0.2161 0.0294  0.0237  0.0358  162 ASP   A N   
3643 C  CA  A ASP   A 162 ? 0.1290 0.3209 0.2550 0.0013  0.0295  0.0891  162 ASP   A CA  
3644 C  CA  B ASP   A 162 ? 0.1774 0.2726 0.2296 0.0216  0.0256  0.0350  162 ASP   A CA  
3645 C  C   A ASP   A 162 ? 0.1224 0.3410 0.2351 -0.0031 0.0267  0.0974  162 ASP   A C   
3646 C  C   B ASP   A 162 ? 0.1785 0.2856 0.2212 0.0109  0.0302  0.0387  162 ASP   A C   
3647 O  O   A ASP   A 162 ? 0.1252 0.3442 0.2400 -0.0027 0.0276  0.0789  162 ASP   A O   
3648 O  O   B ASP   A 162 ? 0.1760 0.2850 0.2135 0.0080  0.0419  0.0349  162 ASP   A O   
3649 C  CB  A ASP   A 162 ? 0.1382 0.3339 0.2990 0.0048  0.0372  0.0622  162 ASP   A CB  
3650 C  CB  B ASP   A 162 ? 0.1843 0.2759 0.2518 0.0238  0.0263  0.0328  162 ASP   A CB  
3651 C  CG  A ASP   A 162 ? 0.1553 0.3509 0.3364 0.0093  0.0393  0.0381  162 ASP   A CG  
3652 C  CG  B ASP   A 162 ? 0.1925 0.2835 0.2751 0.0250  0.0244  0.0300  162 ASP   A CG  
3653 O  OD1 A ASP   A 162 ? 0.1631 0.3556 0.3508 -0.0041 0.0402  0.0329  162 ASP   A OD1 
3654 O  OD1 B ASP   A 162 ? 0.1997 0.2878 0.2845 0.0170  0.0214  0.0235  162 ASP   A OD1 
3655 O  OD2 A ASP   A 162 ? 0.1750 0.3595 0.3552 0.0261  0.0425  0.0234  162 ASP   A OD2 
3656 O  OD2 B ASP   A 162 ? 0.1998 0.2859 0.2933 0.0328  0.0257  0.0329  162 ASP   A OD2 
3665 N  N   A LYS   A 163 ? 0.1264 0.3584 0.2384 -0.0036 0.0018  0.1000  163 LYS   A N   
3666 N  N   B LYS   A 163 ? 0.1849 0.2961 0.2301 0.0064  0.0159  0.0440  163 LYS   A N   
3667 C  CA  A LYS   A 163 ? 0.1411 0.3742 0.2414 -0.0039 0.0056  0.0979  163 LYS   A CA  
3668 C  CA  B LYS   A 163 ? 0.1911 0.3061 0.2396 0.0014  0.0060  0.0448  163 LYS   A CA  
3669 C  C   A LYS   A 163 ? 0.1404 0.3666 0.2296 -0.0098 0.0157  0.0934  163 LYS   A C   
3670 C  C   B LYS   A 163 ? 0.1795 0.3031 0.2231 -0.0006 0.0081  0.0480  163 LYS   A C   
3671 O  O   A LYS   A 163 ? 0.1380 0.3809 0.2373 -0.0199 0.0154  0.0871  163 LYS   A O   
3672 O  O   B LYS   A 163 ? 0.1803 0.3134 0.2172 -0.0012 0.0143  0.0458  163 LYS   A O   
3673 C  CB  A LYS   A 163 ? 0.1766 0.3962 0.2858 0.0143  -0.0081 0.0928  163 LYS   A CB  
3674 C  CB  B LYS   A 163 ? 0.2140 0.3184 0.2798 0.0010  0.0021  0.0385  163 LYS   A CB  
3675 C  CG  A LYS   A 163 ? 0.2185 0.4149 0.3452 0.0212  -0.0040 0.0842  163 LYS   A CG  
3676 C  CG  B LYS   A 163 ? 0.2338 0.3287 0.3173 -0.0009 0.0049  0.0318  163 LYS   A CG  
3677 C  CD  A LYS   A 163 ? 0.2589 0.4284 0.4116 0.0251  -0.0010 0.0741  163 LYS   A CD  
3678 C  CD  B LYS   A 163 ? 0.2486 0.3377 0.3504 -0.0012 0.0073  0.0250  163 LYS   A CD  
3679 C  CE  A LYS   A 163 ? 0.2907 0.4361 0.4612 0.0282  0.0065  0.0720  163 LYS   A CE  
3680 C  CE  B LYS   A 163 ? 0.2593 0.3445 0.3810 -0.0017 0.0076  0.0186  163 LYS   A CE  
3681 N  NZ  A LYS   A 163 ? 0.3087 0.4405 0.4895 0.0292  0.0117  0.0724  163 LYS   A NZ  
3682 N  NZ  B LYS   A 163 ? 0.2640 0.3469 0.3930 -0.0016 0.0089  0.0170  163 LYS   A NZ  
3709 N  N   A LEU   A 164 ? 0.1269 0.3375 0.2121 -0.0167 0.0122  0.0841  164 LEU   A N   
3710 N  N   B LEU   A 164 ? 0.1636 0.2856 0.2133 -0.0045 0.0049  0.0467  164 LEU   A N   
3711 C  CA  A LEU   A 164 ? 0.1404 0.3113 0.1896 -0.0281 0.0192  0.0737  164 LEU   A CA  
3712 C  CA  B LEU   A 164 ? 0.1585 0.2686 0.1997 -0.0118 0.0105  0.0445  164 LEU   A CA  
3713 C  C   A LEU   A 164 ? 0.1548 0.3074 0.1830 -0.0304 0.0152  0.0627  164 LEU   A C   
3714 C  C   B LEU   A 164 ? 0.1600 0.2671 0.1993 -0.0185 0.0140  0.0412  164 LEU   A C   
3715 O  O   A LEU   A 164 ? 0.1597 0.3138 0.1892 -0.0385 0.0280  0.0524  164 LEU   A O   
3716 O  O   B LEU   A 164 ? 0.1602 0.2720 0.2049 -0.0245 0.0187  0.0384  164 LEU   A O   
3717 C  CB  A LEU   A 164 ? 0.1431 0.2926 0.1846 -0.0252 0.0152  0.0723  164 LEU   A CB  
3718 C  CB  B LEU   A 164 ? 0.1560 0.2551 0.1889 -0.0096 0.0158  0.0424  164 LEU   A CB  
3719 C  CG  A LEU   A 164 ? 0.1481 0.2781 0.1876 -0.0196 0.0090  0.0650  164 LEU   A CG  
3720 C  CG  B LEU   A 164 ? 0.1565 0.2447 0.1865 -0.0029 0.0198  0.0400  164 LEU   A CG  
3721 C  CD1 A LEU   A 164 ? 0.1411 0.2696 0.1884 -0.0148 -0.0029 0.0669  164 LEU   A CD1 
3722 C  CD1 B LEU   A 164 ? 0.1538 0.2422 0.1847 0.0033  0.0243  0.0345  164 LEU   A CD1 
3723 C  CD2 A LEU   A 164 ? 0.1688 0.2771 0.1895 -0.0219 0.0185  0.0535  164 LEU   A CD2 
3724 C  CD2 B LEU   A 164 ? 0.1593 0.2394 0.1846 -0.0068 0.0247  0.0363  164 LEU   A CD2 
3747 N  N   A VAL   A 165 ? 0.1507 0.2973 0.1696 -0.0295 0.0137  0.0668  165 VAL   A N   
3748 N  N   B VAL   A 165 ? 0.1589 0.2628 0.1996 -0.0202 0.0116  0.0376  165 VAL   A N   
3749 C  CA  A VAL   A 165 ? 0.1611 0.2955 0.1623 -0.0278 0.0160  0.0722  165 VAL   A CA  
3750 C  CA  B VAL   A 165 ? 0.1632 0.2625 0.2034 -0.0214 0.0139  0.0395  165 VAL   A CA  
3751 C  C   A VAL   A 165 ? 0.1455 0.3077 0.1665 -0.0216 0.0252  0.0728  165 VAL   A C   
3752 C  C   B VAL   A 165 ? 0.1585 0.2690 0.2062 -0.0200 0.0141  0.0385  165 VAL   A C   
3753 O  O   A VAL   A 165 ? 0.1412 0.3090 0.1754 -0.0262 0.0286  0.0697  165 VAL   A O   
3754 O  O   B VAL   A 165 ? 0.1574 0.2692 0.2001 -0.0220 0.0185  0.0363  165 VAL   A O   
3755 C  CB  A VAL   A 165 ? 0.1845 0.2879 0.1760 -0.0288 0.0209  0.0668  165 VAL   A CB  
3756 C  CB  B VAL   A 165 ? 0.1708 0.2574 0.2083 -0.0193 0.0120  0.0342  165 VAL   A CB  
3757 C  CG1 A VAL   A 165 ? 0.1898 0.2924 0.1839 -0.0300 0.0265  0.0543  165 VAL   A CG1 
3758 C  CG1 B VAL   A 165 ? 0.1711 0.2567 0.2113 -0.0197 0.0144  0.0328  165 VAL   A CG1 
3759 C  CG2 A VAL   A 165 ? 0.1962 0.2873 0.1888 -0.0272 0.0134  0.0695  165 VAL   A CG2 
3760 C  CG2 B VAL   A 165 ? 0.1765 0.2574 0.2129 -0.0191 0.0070  0.0327  165 VAL   A CG2 
3779 N  N   A SER   A 166 ? 0.1375 0.3201 0.1891 -0.0163 0.0164  0.0604  166 SER   A N   
3780 N  N   B SER   A 166 ? 0.1532 0.2753 0.2149 -0.0203 0.0112  0.0387  166 SER   A N   
3781 C  CA  A SER   A 166 ? 0.1436 0.3362 0.2101 -0.0180 0.0204  0.0520  166 SER   A CA  
3782 C  CA  B SER   A 166 ? 0.1527 0.2823 0.2149 -0.0252 0.0119  0.0421  166 SER   A CA  
3783 C  C   A SER   A 166 ? 0.1526 0.3522 0.2155 -0.0136 0.0063  0.0468  166 SER   A C   
3784 C  C   B SER   A 166 ? 0.1653 0.2921 0.2158 -0.0322 0.0130  0.0484  166 SER   A C   
3785 O  O   A SER   A 166 ? 0.1745 0.3667 0.2330 -0.0261 -0.0071 0.0239  166 SER   A O   
3786 O  O   B SER   A 166 ? 0.1691 0.3000 0.2093 -0.0360 0.0164  0.0482  166 SER   A O   
3787 C  CB  A SER   A 166 ? 0.1516 0.3366 0.2303 -0.0163 0.0175  0.0478  166 SER   A CB  
3788 C  CB  B SER   A 166 ? 0.1439 0.2795 0.2210 -0.0195 0.0021  0.0382  166 SER   A CB  
3789 O  OG  A SER   A 166 ? 0.1677 0.3378 0.2508 -0.0128 0.0170  0.0542  166 SER   A OG  
3790 O  OG  B SER   A 166 ? 0.1435 0.2762 0.2299 -0.0111 -0.0084 0.0412  166 SER   A OG  
3801 N  N   A SER   A 167 ? 0.1535 0.3490 0.1860 0.0084  0.0046  0.0640  167 SER   A N   
3802 N  N   B SER   A 167 ? 0.1798 0.2919 0.2358 -0.0283 0.0139  0.0502  167 SER   A N   
3803 C  CA  A SER   A 167 ? 0.1719 0.3465 0.1885 0.0119  -0.0048 0.0510  167 SER   A CA  
3804 C  CA  B SER   A 167 ? 0.1969 0.2934 0.2578 -0.0254 0.0155  0.0439  167 SER   A CA  
3805 C  C   A SER   A 167 ? 0.1732 0.3319 0.1970 0.0210  0.0089  0.0403  167 SER   A C   
3806 C  C   B SER   A 167 ? 0.1982 0.2904 0.2673 -0.0158 0.0236  0.0332  167 SER   A C   
3807 O  O   A SER   A 167 ? 0.1838 0.3352 0.1958 0.0211  0.0048  0.0303  167 SER   A O   
3808 O  O   B SER   A 167 ? 0.2159 0.2981 0.2896 -0.0161 0.0201  0.0276  167 SER   A O   
3809 C  CB  A SER   A 167 ? 0.1682 0.3551 0.2048 0.0035  0.0083  0.0444  167 SER   A CB  
3810 C  CB  B SER   A 167 ? 0.2071 0.2989 0.2714 -0.0274 0.0122  0.0435  167 SER   A CB  
3811 O  OG  A SER   A 167 ? 0.1483 0.3634 0.2098 0.0001  0.0296  0.0466  167 SER   A OG  
3812 O  OG  B SER   A 167 ? 0.2170 0.3048 0.2881 -0.0256 0.0024  0.0447  167 SER   A OG  
3823 N  N   A PHE   A 168 ? 0.1622 0.3130 0.2043 0.0286  0.0146  0.0409  168 PHE   A N   
3824 N  N   B PHE   A 168 ? 0.1775 0.2789 0.2441 -0.0083 0.0382  0.0301  168 PHE   A N   
3825 C  CA  A PHE   A 168 ? 0.1645 0.3020 0.2313 0.0179  0.0233  0.0404  168 PHE   A CA  
3826 C  CA  B PHE   A 168 ? 0.1694 0.2745 0.2234 -0.0017 0.0491  0.0267  168 PHE   A CA  
3827 C  C   A PHE   A 168 ? 0.1784 0.3047 0.2834 0.0048  0.0491  0.0345  168 PHE   A C   
3828 C  C   B PHE   A 168 ? 0.1738 0.2746 0.2296 -0.0030 0.0517  0.0241  168 PHE   A C   
3829 O  O   A PHE   A 168 ? 0.1893 0.3100 0.3273 -0.0026 0.0544  0.0461  168 PHE   A O   
3830 O  O   B PHE   A 168 ? 0.1641 0.2729 0.2199 -0.0004 0.0658  0.0250  168 PHE   A O   
3831 C  CB  A PHE   A 168 ? 0.1637 0.2957 0.2206 0.0071  0.0086  0.0388  168 PHE   A CB  
3832 C  CB  B PHE   A 168 ? 0.1718 0.2731 0.2197 -0.0038 0.0450  0.0312  168 PHE   A CB  
3833 C  CG  A PHE   A 168 ? 0.1587 0.2926 0.2033 0.0002  0.0056  0.0371  168 PHE   A CG  
3834 C  CG  B PHE   A 168 ? 0.1737 0.2688 0.2095 -0.0048 0.0407  0.0405  168 PHE   A CG  
3835 C  CD1 A PHE   A 168 ? 0.1588 0.2954 0.2054 -0.0037 0.0017  0.0407  168 PHE   A CD1 
3836 C  CD1 B PHE   A 168 ? 0.1751 0.2693 0.2101 -0.0055 0.0414  0.0480  168 PHE   A CD1 
3837 C  CD2 A PHE   A 168 ? 0.1555 0.2905 0.1950 -0.0048 0.0127  0.0351  168 PHE   A CD2 
3838 C  CD2 B PHE   A 168 ? 0.1784 0.2646 0.2119 -0.0025 0.0285  0.0447  168 PHE   A CD2 
3839 C  CE1 A PHE   A 168 ? 0.1481 0.2910 0.1929 -0.0065 0.0052  0.0418  168 PHE   A CE1 
3840 C  CE1 B PHE   A 168 ? 0.1769 0.2672 0.2131 -0.0041 0.0353  0.0544  168 PHE   A CE1 
3841 C  CE2 A PHE   A 168 ? 0.1622 0.2862 0.1962 -0.0052 0.0115  0.0410  168 PHE   A CE2 
3842 C  CE2 B PHE   A 168 ? 0.1830 0.2633 0.2128 -0.0019 0.0239  0.0532  168 PHE   A CE2 
3843 C  CZ  A PHE   A 168 ? 0.1545 0.2871 0.1898 -0.0054 0.0101  0.0386  168 PHE   A CZ  
3844 C  CZ  B PHE   A 168 ? 0.1816 0.2641 0.2123 -0.0031 0.0302  0.0540  168 PHE   A CZ  
3863 N  N   A LEU   A 169 ? 0.2073 0.3023 0.3104 -0.0059 0.0549  0.0145  169 LEU   A N   
3864 N  N   B LEU   A 169 ? 0.1848 0.2773 0.2445 -0.0049 0.0436  0.0211  169 LEU   A N   
3865 C  CA  A LEU   A 169 ? 0.2447 0.3085 0.3567 -0.0112 0.0406  0.0071  169 LEU   A CA  
3866 C  CA  B LEU   A 169 ? 0.2010 0.2841 0.2676 -0.0087 0.0288  0.0132  169 LEU   A CA  
3867 C  C   A LEU   A 169 ? 0.2413 0.3020 0.3734 -0.0137 0.0481  0.0230  169 LEU   A C   
3868 C  C   B LEU   A 169 ? 0.2159 0.2916 0.2807 -0.0042 0.0226  0.0061  169 LEU   A C   
3869 O  O   A LEU   A 169 ? 0.2423 0.3041 0.3857 -0.0126 0.0410  0.0224  169 LEU   A O   
3870 O  O   B LEU   A 169 ? 0.2275 0.2977 0.2915 -0.0039 0.0233  0.0081  169 LEU   A O   
3871 C  CB  A LEU   A 169 ? 0.2748 0.3207 0.3597 -0.0116 0.0371  -0.0134 169 LEU   A CB  
3872 C  CB  B LEU   A 169 ? 0.2030 0.2852 0.2703 -0.0144 0.0216  0.0158  169 LEU   A CB  
3873 C  CG  A LEU   A 169 ? 0.3016 0.3320 0.3654 -0.0140 0.0329  -0.0388 169 LEU   A CG  
3874 C  CG  B LEU   A 169 ? 0.2039 0.2854 0.2697 -0.0198 0.0197  0.0201  169 LEU   A CG  
3875 C  CD1 A LEU   A 169 ? 0.3099 0.3341 0.3695 -0.0139 0.0285  -0.0459 169 LEU   A CD1 
3876 C  CD1 B LEU   A 169 ? 0.2053 0.2884 0.2825 -0.0240 0.0132  0.0194  169 LEU   A CD1 
3877 C  CD2 A LEU   A 169 ? 0.3106 0.3370 0.3608 -0.0171 0.0325  -0.0479 169 LEU   A CD2 
3878 C  CD2 B LEU   A 169 ? 0.2079 0.2855 0.2678 -0.0222 0.0236  0.0222  169 LEU   A CD2 
3879 O  OXT A LEU   A 169 ? 0.2250 0.3011 0.3650 -0.0179 0.0667  0.0299  169 LEU   A OXT 
3880 O  OXT B LEU   A 169 ? 0.2178 0.2939 0.2823 -0.0042 0.0159  0.0002  169 LEU   A OXT 
3903 N  N   A SER   B 1   ? 0.3771 0.3335 0.3443 -0.1108 -0.0749 0.0323  1   SER   B N   
3904 N  N   B SER   B 1   ? 0.3415 0.3365 0.3410 -0.0816 -0.0508 0.0289  1   SER   B N   
3905 C  CA  A SER   B 1   ? 0.3694 0.3404 0.3578 -0.1189 -0.0770 0.0289  1   SER   B CA  
3906 C  CA  B SER   B 1   ? 0.3369 0.3391 0.3448 -0.0849 -0.0508 0.0294  1   SER   B CA  
3907 C  C   A SER   B 1   ? 0.3415 0.3444 0.3433 -0.1230 -0.0862 0.0479  1   SER   B C   
3908 C  C   B SER   B 1   ? 0.3212 0.3384 0.3343 -0.0860 -0.0592 0.0452  1   SER   B C   
3909 O  O   A SER   B 1   ? 0.3509 0.3498 0.3190 -0.1174 -0.0797 0.0475  1   SER   B O   
3910 O  O   B SER   B 1   ? 0.3258 0.3406 0.3227 -0.0838 -0.0561 0.0418  1   SER   B O   
3911 C  CB  A SER   B 1   ? 0.3837 0.3381 0.3700 -0.1212 -0.0693 0.0111  1   SER   B CB  
3912 C  CB  B SER   B 1   ? 0.3436 0.3394 0.3508 -0.0858 -0.0426 0.0177  1   SER   B CB  
3913 O  OG  A SER   B 1   ? 0.3992 0.3483 0.4175 -0.1168 -0.0655 0.0051  1   SER   B OG  
3914 O  OG  B SER   B 1   ? 0.3505 0.3445 0.3747 -0.0854 -0.0396 0.0126  1   SER   B OG  
3929 N  N   A MET   B 2   ? 0.3135 0.3429 0.3433 -0.1215 -0.0893 0.0851  2   MET   B N   
3930 N  N   B MET   B 2   ? 0.3036 0.3351 0.3283 -0.0856 -0.0660 0.0745  2   MET   B N   
3931 C  CA  A MET   B 2   ? 0.2940 0.3463 0.3583 -0.1002 -0.0910 0.1093  2   MET   B CA  
3932 C  CA  B MET   B 2   ? 0.2874 0.3330 0.3282 -0.0773 -0.0734 0.1002  2   MET   B CA  
3933 C  C   A MET   B 2   ? 0.2587 0.3305 0.3256 -0.0769 -0.1016 0.1359  2   MET   B C   
3934 C  C   B MET   B 2   ? 0.2605 0.3193 0.3126 -0.0745 -0.0837 0.1249  2   MET   B C   
3935 O  O   A MET   B 2   ? 0.2543 0.3446 0.3278 -0.0571 -0.1133 0.1396  2   MET   B O   
3936 O  O   B MET   B 2   ? 0.2602 0.3244 0.3126 -0.0684 -0.0851 0.1233  2   MET   B O   
3937 C  CB  A MET   B 2   ? 0.3227 0.3764 0.4383 -0.0836 -0.0672 0.0869  2   MET   B CB  
3938 C  CB  B MET   B 2   ? 0.3023 0.3491 0.3589 -0.0641 -0.0651 0.0944  2   MET   B CB  
3939 C  CG  A MET   B 2   ? 0.3502 0.4044 0.5101 -0.0637 -0.0440 0.0720  2   MET   B CG  
3940 C  CG  B MET   B 2   ? 0.3154 0.3642 0.3821 -0.0493 -0.0582 0.0973  2   MET   B CG  
3941 S  SD  A MET   B 2   ? 0.3763 0.4314 0.5841 -0.0449 -0.0294 0.0606  2   MET   B SD  
3942 S  SD  B MET   B 2   ? 0.3272 0.3804 0.3991 -0.0347 -0.0562 0.1023  2   MET   B SD  
3943 C  CE  A MET   B 2   ? 0.3805 0.4374 0.5829 -0.0432 -0.0241 0.0628  2   MET   B CE  
3944 C  CE  B MET   B 2   ? 0.3296 0.3838 0.4064 -0.0333 -0.0537 0.0956  2   MET   B CE  
3963 N  N   . VAL   B 3   ? 0.2357 0.2992 0.3072 -0.0790 -0.0880 0.1467  3   VAL   B N   
3964 C  CA  . VAL   B 3   ? 0.2212 0.2631 0.3026 -0.0691 -0.0810 0.1287  3   VAL   B CA  
3965 C  C   . VAL   B 3   ? 0.2001 0.2516 0.2630 -0.0660 -0.0727 0.1116  3   VAL   B C   
3966 O  O   . VAL   B 3   ? 0.1981 0.2694 0.2717 -0.0695 -0.0682 0.1215  3   VAL   B O   
3967 C  CB  . VAL   B 3   ? 0.2358 0.2530 0.3518 -0.0699 -0.0703 0.1132  3   VAL   B CB  
3968 C  CG1 . VAL   B 3   ? 0.2465 0.2441 0.3760 -0.0727 -0.0645 0.1110  3   VAL   B CG1 
3969 C  CG2 . VAL   B 3   ? 0.2383 0.2603 0.3677 -0.0625 -0.0611 0.1176  3   VAL   B CG2 
3980 N  N   . ASN   B 4   ? 0.1880 0.2213 0.2341 -0.0600 -0.0631 0.0839  4   ASN   B N   
3981 C  CA  . ASN   B 4   ? 0.1868 0.2187 0.2006 -0.0598 -0.0480 0.0507  4   ASN   B CA  
3982 C  C   . ASN   B 4   ? 0.1873 0.2367 0.1970 -0.0611 -0.0372 0.0369  4   ASN   B C   
3983 O  O   . ASN   B 4   ? 0.1898 0.2418 0.2169 -0.0552 -0.0303 0.0206  4   ASN   B O   
3984 C  CB  . ASN   B 4   ? 0.1902 0.2109 0.1826 -0.0557 -0.0651 0.0379  4   ASN   B CB  
3985 C  CG  . ASN   B 4   ? 0.1913 0.1990 0.1749 -0.0541 -0.0590 0.0307  4   ASN   B CG  
3986 O  OD1 . ASN   B 4   ? 0.1962 0.1859 0.1816 -0.0572 -0.0528 0.0314  4   ASN   B OD1 
3987 N  ND2 . ASN   B 4   ? 0.2086 0.2049 0.1942 -0.0374 -0.0381 0.0229  4   ASN   B ND2 
3994 N  N   . SER   B 5   ? 0.2015 0.2561 0.2032 -0.0656 -0.0363 0.0351  5   SER   B N   
3995 C  CA  . SER   B 5   ? 0.2322 0.2924 0.2282 -0.0600 -0.0187 0.0352  5   SER   B CA  
3996 C  C   . SER   B 5   ? 0.2589 0.2997 0.2567 -0.0763 0.0117  0.0376  5   SER   B C   
3997 O  O   . SER   B 5   ? 0.2818 0.2947 0.3204 -0.0653 0.0484  0.0327  5   SER   B O   
3998 C  CB  . SER   B 5   ? 0.2479 0.3139 0.2589 -0.0475 -0.0045 0.0407  5   SER   B CB  
3999 O  OG  . SER   B 5   ? 0.2720 0.3368 0.3182 -0.0323 0.0037  0.0410  5   SER   B OG  
4005 N  N   . PHE   B 6   ? 0.2804 0.3212 0.2484 -0.0861 0.0267  0.0465  6   PHE   B N   
4006 C  CA  . PHE   B 6   ? 0.2929 0.3293 0.2238 -0.1051 0.0329  0.0261  6   PHE   B CA  
4007 C  C   . PHE   B 6   ? 0.3531 0.3742 0.2652 -0.1130 0.0616  -0.0007 6   PHE   B C   
4008 O  O   . PHE   B 6   ? 0.3688 0.4049 0.3016 -0.1040 0.0457  -0.0178 6   PHE   B O   
4009 C  CB  . PHE   B 6   ? 0.2588 0.3024 0.1984 -0.0910 0.0126  0.0212  6   PHE   B CB  
4010 C  CG  . PHE   B 6   ? 0.2236 0.2671 0.1859 -0.0838 -0.0038 0.0247  6   PHE   B CG  
4011 C  CD1 . PHE   B 6   ? 0.2262 0.2411 0.1759 -0.0726 -0.0154 0.0208  6   PHE   B CD1 
4012 C  CD2 . PHE   B 6   ? 0.1989 0.2651 0.1759 -0.0715 -0.0084 0.0513  6   PHE   B CD2 
4013 C  CE1 . PHE   B 6   ? 0.2208 0.2195 0.1767 -0.0644 -0.0186 0.0134  6   PHE   B CE1 
4014 C  CE2 . PHE   B 6   ? 0.2058 0.2516 0.2110 -0.0600 -0.0024 0.0377  6   PHE   B CE2 
4015 C  CZ  . PHE   B 6   ? 0.2102 0.2269 0.1919 -0.0604 -0.0104 0.0175  6   PHE   B CZ  
4025 N  N   . SER   B 7   ? 0.3955 0.3706 0.2847 -0.1343 0.1055  -0.0191 7   SER   B N   
4026 C  CA  . SER   B 7   ? 0.4353 0.3924 0.3438 -0.1359 0.1323  -0.0265 7   SER   B CA  
4027 C  C   . SER   B 7   ? 0.4325 0.3641 0.3153 -0.1400 0.1430  -0.0465 7   SER   B C   
4028 O  O   . SER   B 7   ? 0.4384 0.3601 0.3366 -0.1467 0.1345  -0.0501 7   SER   B O   
4029 C  CB  . SER   B 7   ? 0.4671 0.4346 0.4262 -0.1329 0.1520  -0.0121 7   SER   B CB  
4030 O  OG  . SER   B 7   ? 0.4739 0.4494 0.4860 -0.1323 0.1595  0.0007  7   SER   B OG  
4036 N  N   . GLY   B 8   ? 0.4299 0.3481 0.3070 -0.1245 0.1493  -0.0619 8   GLY   B N   
4037 C  CA  . GLY   B 8   ? 0.4167 0.3269 0.3036 -0.1121 0.1446  -0.0732 8   GLY   B CA  
4038 C  C   . GLY   B 8   ? 0.3922 0.2935 0.2970 -0.1066 0.1362  -0.0716 8   GLY   B C   
4039 O  O   . GLY   B 8   ? 0.4017 0.3003 0.3287 -0.0950 0.1370  -0.0794 8   GLY   B O   
4043 N  N   . TYR   B 9   ? 0.3707 0.2627 0.2694 -0.0957 0.1092  -0.0778 9   TYR   B N   
4044 C  CA  . TYR   B 9   ? 0.3459 0.2290 0.2406 -0.0841 0.0839  -0.0565 9   TYR   B CA  
4045 C  C   . TYR   B 9   ? 0.3420 0.2233 0.2337 -0.0795 0.0537  -0.0390 9   TYR   B C   
4046 O  O   . TYR   B 9   ? 0.3537 0.2393 0.2737 -0.0795 0.0563  -0.0300 9   TYR   B O   
4047 C  CB  . TYR   B 9   ? 0.3325 0.2007 0.2480 -0.0769 0.0823  -0.0541 9   TYR   B CB  
4048 C  CG  . TYR   B 9   ? 0.3219 0.1838 0.2501 -0.0826 0.0706  -0.0537 9   TYR   B CG  
4049 C  CD1 . TYR   B 9   ? 0.3263 0.1842 0.2555 -0.0934 0.0697  -0.0473 9   TYR   B CD1 
4050 C  CD2 . TYR   B 9   ? 0.3085 0.1870 0.2383 -0.0737 0.0648  -0.0574 9   TYR   B CD2 
4051 C  CE1 . TYR   B 9   ? 0.3223 0.1975 0.2538 -0.0969 0.0723  -0.0566 9   TYR   B CE1 
4052 C  CE2 . TYR   B 9   ? 0.3101 0.1891 0.2428 -0.0765 0.0653  -0.0503 9   TYR   B CE2 
4053 C  CZ  . TYR   B 9   ? 0.3141 0.1988 0.2539 -0.0906 0.0698  -0.0608 9   TYR   B CZ  
4054 O  OH  . TYR   B 9   ? 0.3115 0.2113 0.2683 -0.0979 0.0718  -0.0774 9   TYR   B OH  
4064 N  N   . LEU   B 10  ? 0.3232 0.1988 0.2108 -0.0808 0.0279  -0.0389 10  LEU   B N   
4065 C  CA  . LEU   B 10  ? 0.3173 0.2000 0.2163 -0.0889 -0.0121 -0.0341 10  LEU   B CA  
4066 C  C   . LEU   B 10  ? 0.2982 0.2000 0.2288 -0.0823 -0.0307 -0.0272 10  LEU   B C   
4067 O  O   . LEU   B 10  ? 0.2790 0.2010 0.2377 -0.0702 -0.0239 -0.0221 10  LEU   B O   
4068 C  CB  . LEU   B 10  ? 0.3346 0.2004 0.2325 -0.0922 -0.0223 -0.0161 10  LEU   B CB  
4069 C  CG  . LEU   B 10  ? 0.3543 0.2150 0.2592 -0.0855 -0.0474 -0.0098 10  LEU   B CG  
4070 C  CD1 . LEU   B 10  ? 0.3674 0.2249 0.2756 -0.0841 -0.0411 -0.0073 10  LEU   B CD1 
4071 C  CD2 . LEU   B 10  ? 0.3633 0.2225 0.2861 -0.0830 -0.0484 0.0098  10  LEU   B CD2 
4083 N  N   . LYS   B 11  ? 0.3102 0.2245 0.2310 -0.0744 -0.0391 -0.0192 11  LYS   B N   
4084 C  CA  . LYS   B 11  ? 0.3263 0.2507 0.2718 -0.0573 -0.0475 -0.0271 11  LYS   B CA  
4085 C  C   . LYS   B 11  ? 0.3071 0.2277 0.2754 -0.0774 -0.0410 -0.0364 11  LYS   B C   
4086 O  O   . LYS   B 11  ? 0.3185 0.2419 0.3085 -0.0955 -0.0387 -0.0743 11  LYS   B O   
4087 C  CB  . LYS   B 11  ? 0.3562 0.3000 0.3356 -0.0274 -0.0521 -0.0313 11  LYS   B CB  
4088 C  CG  . LYS   B 11  ? 0.3828 0.3337 0.4056 -0.0086 -0.0501 -0.0285 11  LYS   B CG  
4089 C  CD  . LYS   B 11  ? 0.4040 0.3539 0.4658 0.0009  -0.0471 -0.0280 11  LYS   B CD  
4090 C  CE  . LYS   B 11  ? 0.4194 0.3678 0.5126 0.0014  -0.0501 -0.0303 11  LYS   B CE  
4091 N  NZ  . LYS   B 11  ? 0.4289 0.3760 0.5360 0.0001  -0.0547 -0.0294 11  LYS   B NZ  
4105 N  N   . LEU   B 12  ? 0.2720 0.2030 0.2649 -0.0706 -0.0426 -0.0328 12  LEU   B N   
4106 C  CA  . LEU   B 12  ? 0.2514 0.1844 0.2730 -0.0586 -0.0348 -0.0259 12  LEU   B CA  
4107 C  C   . LEU   B 12  ? 0.2341 0.1831 0.2790 -0.0627 -0.0520 -0.0214 12  LEU   B C   
4108 O  O   . LEU   B 12  ? 0.2304 0.1808 0.2951 -0.0709 -0.0617 -0.0146 12  LEU   B O   
4109 C  CB  . LEU   B 12  ? 0.2466 0.1643 0.2710 -0.0473 -0.0298 -0.0274 12  LEU   B CB  
4110 C  CG  . LEU   B 12  ? 0.2407 0.1594 0.2673 -0.0472 -0.0141 -0.0151 12  LEU   B CG  
4111 C  CD1 . LEU   B 12  ? 0.2485 0.1609 0.2617 -0.0292 -0.0152 0.0034  12  LEU   B CD1 
4112 C  CD2 . LEU   B 12  ? 0.2475 0.1654 0.2748 -0.0426 -0.0109 -0.0275 12  LEU   B CD2 
4124 N  N   . THR   B 13  ? 0.2261 0.1881 0.2773 -0.0618 -0.0572 -0.0326 13  THR   B N   
4125 C  CA  . THR   B 13  ? 0.2248 0.1998 0.2739 -0.0653 -0.0665 -0.0166 13  THR   B CA  
4126 C  C   . THR   B 13  ? 0.2642 0.2183 0.2906 -0.0762 -0.0785 -0.0101 13  THR   B C   
4127 O  O   . THR   B 13  ? 0.2842 0.2188 0.3040 -0.0727 -0.0463 -0.0158 13  THR   B O   
4128 C  CB  . THR   B 13  ? 0.2008 0.1999 0.2790 -0.0598 -0.0596 -0.0074 13  THR   B CB  
4129 O  OG1 . THR   B 13  ? 0.1952 0.1902 0.2950 -0.0497 -0.0514 -0.0141 13  THR   B OG1 
4130 C  CG2 . THR   B 13  ? 0.2026 0.2071 0.2897 -0.0542 -0.0438 0.0060  13  THR   B CG2 
4138 N  N   A ASP   B 14  ? 0.2775 0.2312 0.3039 -0.0830 -0.1056 0.0060  14  ASP   B N   
4139 N  N   B ASP   B 14  ? 0.2729 0.2271 0.2998 -0.0761 -0.0854 0.0004  14  ASP   B N   
4140 C  CA  A ASP   B 14  ? 0.2899 0.2438 0.3291 -0.0855 -0.1076 0.0248  14  ASP   B CA  
4141 C  CA  B ASP   B 14  ? 0.2813 0.2357 0.3143 -0.0743 -0.0821 0.0116  14  ASP   B CA  
4142 C  C   A ASP   B 14  ? 0.2804 0.2255 0.2932 -0.0867 -0.0910 0.0253  14  ASP   B C   
4143 C  C   B ASP   B 14  ? 0.2694 0.2194 0.2852 -0.0753 -0.0821 0.0153  14  ASP   B C   
4144 O  O   A ASP   B 14  ? 0.3068 0.2386 0.2985 -0.0886 -0.0879 0.0337  14  ASP   B O   
4145 O  O   B ASP   B 14  ? 0.2819 0.2233 0.2832 -0.0738 -0.0847 0.0185  14  ASP   B O   
4146 C  CB  A ASP   B 14  ? 0.3105 0.2792 0.4009 -0.0828 -0.1183 0.0237  14  ASP   B CB  
4147 C  CB  B ASP   B 14  ? 0.3004 0.2614 0.3620 -0.0703 -0.0767 0.0126  14  ASP   B CB  
4148 C  CG  A ASP   B 14  ? 0.3369 0.3133 0.4749 -0.0717 -0.1124 0.0087  14  ASP   B CG  
4149 C  CG  B ASP   B 14  ? 0.3194 0.2843 0.4075 -0.0633 -0.0689 0.0073  14  ASP   B CG  
4150 O  OD1 A ASP   B 14  ? 0.3527 0.3218 0.4957 -0.0705 -0.1115 -0.0054 14  ASP   B OD1 
4151 O  OD1 B ASP   B 14  ? 0.3291 0.2939 0.4194 -0.0613 -0.0630 0.0045  14  ASP   B OD1 
4152 O  OD2 A ASP   B 14  ? 0.3396 0.3265 0.5099 -0.0685 -0.1069 0.0093  14  ASP   B OD2 
4153 O  OD2 B ASP   B 14  ? 0.3229 0.2918 0.4253 -0.0629 -0.0691 0.0060  14  ASP   B OD2 
4162 N  N   . ASN   B 15  ? 0.2443 0.1995 0.2690 -0.0723 -0.0828 0.0199  15  ASN   B N   
4163 C  CA  . ASN   B 15  ? 0.1969 0.1708 0.2538 -0.0482 -0.0637 0.0106  15  ASN   B CA  
4164 C  C   . ASN   B 15  ? 0.1798 0.1542 0.2348 -0.0304 -0.0531 -0.0008 15  ASN   B C   
4165 O  O   . ASN   B 15  ? 0.1766 0.1484 0.2473 -0.0289 -0.0511 -0.0137 15  ASN   B O   
4166 C  CB  . ASN   B 15  ? 0.1916 0.1680 0.2718 -0.0284 -0.0673 0.0093  15  ASN   B CB  
4167 C  CG  . ASN   B 15  ? 0.1727 0.1619 0.2667 -0.0296 -0.0395 0.0171  15  ASN   B CG  
4168 O  OD1 . ASN   B 15  ? 0.1779 0.1907 0.2973 -0.0518 -0.0382 0.0211  15  ASN   B OD1 
4169 N  ND2 . ASN   B 15  ? 0.1671 0.1396 0.2600 -0.0166 -0.0107 -0.0035 15  ASN   B ND2 
4177 N  N   . VAL   B 16  ? 0.1801 0.1507 0.2364 -0.0368 -0.0605 -0.0047 16  VAL   B N   
4178 C  CA  . VAL   B 16  ? 0.1791 0.1549 0.2229 -0.0346 -0.0425 -0.0202 16  VAL   B CA  
4179 C  C   . VAL   B 16  ? 0.1819 0.1681 0.2246 -0.0411 -0.0436 -0.0129 16  VAL   B C   
4180 O  O   . VAL   B 16  ? 0.1846 0.1767 0.2420 -0.0373 -0.0408 -0.0220 16  VAL   B O   
4181 C  CB  . VAL   B 16  ? 0.1801 0.1530 0.2339 -0.0194 -0.0307 -0.0204 16  VAL   B CB  
4182 C  CG1 . VAL   B 16  ? 0.1870 0.1505 0.2288 -0.0038 -0.0328 -0.0157 16  VAL   B CG1 
4183 C  CG2 . VAL   B 16  ? 0.1831 0.1570 0.2525 -0.0165 -0.0286 -0.0139 16  VAL   B CG2 
4193 N  N   . TYR   B 17  ? 0.1861 0.1726 0.2168 -0.0358 -0.0383 -0.0185 17  TYR   B N   
4194 C  CA  . TYR   B 17  ? 0.1938 0.1852 0.2143 -0.0477 -0.0295 0.0007  17  TYR   B CA  
4195 C  C   . TYR   B 17  ? 0.1864 0.1572 0.2058 -0.0491 -0.0216 -0.0059 17  TYR   B C   
4196 O  O   . TYR   B 17  ? 0.1804 0.1656 0.2177 -0.0400 -0.0255 -0.0321 17  TYR   B O   
4197 C  CB  . TYR   B 17  ? 0.2254 0.2318 0.2348 -0.0332 -0.0297 0.0349  17  TYR   B CB  
4198 C  CG  . TYR   B 17  ? 0.2533 0.2874 0.2699 -0.0252 -0.0466 0.0478  17  TYR   B CG  
4199 C  CD1 . TYR   B 17  ? 0.2713 0.3053 0.2970 -0.0229 -0.0556 0.0570  17  TYR   B CD1 
4200 C  CD2 . TYR   B 17  ? 0.2748 0.3148 0.2958 -0.0154 -0.0574 0.0466  17  TYR   B CD2 
4201 C  CE1 . TYR   B 17  ? 0.2887 0.3293 0.3144 -0.0124 -0.0663 0.0507  17  TYR   B CE1 
4202 C  CE2 . TYR   B 17  ? 0.2902 0.3340 0.3156 -0.0031 -0.0719 0.0524  17  TYR   B CE2 
4203 C  CZ  . TYR   B 17  ? 0.3002 0.3465 0.3262 -0.0008 -0.0767 0.0518  17  TYR   B CZ  
4204 O  OH  . TYR   B 17  ? 0.3159 0.3605 0.3439 0.0082  -0.0845 0.0525  17  TYR   B OH  
4214 N  N   . ILE   B 18  ? 0.2004 0.1575 0.2024 -0.0418 -0.0132 -0.0154 18  ILE   B N   
4215 C  CA  . ILE   B 18  ? 0.2031 0.1533 0.2012 -0.0432 -0.0112 -0.0227 18  ILE   B CA  
4216 C  C   . ILE   B 18  ? 0.2138 0.1603 0.1955 -0.0531 -0.0064 -0.0326 18  ILE   B C   
4217 O  O   . ILE   B 18  ? 0.2335 0.1739 0.2081 -0.0496 0.0014  -0.0343 18  ILE   B O   
4218 C  CB  . ILE   B 18  ? 0.2078 0.1576 0.2088 -0.0472 -0.0114 -0.0165 18  ILE   B CB  
4219 C  CG1 . ILE   B 18  ? 0.2060 0.1676 0.2165 -0.0480 -0.0075 -0.0084 18  ILE   B CG1 
4220 C  CG2 . ILE   B 18  ? 0.2120 0.1616 0.2182 -0.0477 -0.0151 -0.0130 18  ILE   B CG2 
4221 C  CD1 . ILE   B 18  ? 0.2117 0.1952 0.2353 -0.0396 -0.0247 0.0180  18  ILE   B CD1 
4233 N  N   . LYS   B 19  ? 0.2140 0.1620 0.2124 -0.0304 0.0288  -0.0392 19  LYS   B N   
4234 C  CA  . LYS   B 19  ? 0.2193 0.1654 0.2378 -0.0342 0.0296  -0.0447 19  LYS   B CA  
4235 C  C   . LYS   B 19  ? 0.2012 0.1642 0.2494 -0.0306 0.0326  -0.0540 19  LYS   B C   
4236 O  O   . LYS   B 19  ? 0.1925 0.1662 0.2318 -0.0236 0.0266  -0.0431 19  LYS   B O   
4237 C  CB  . LYS   B 19  ? 0.2456 0.1878 0.2478 -0.0386 0.0352  -0.0348 19  LYS   B CB  
4238 C  CG  . LYS   B 19  ? 0.2719 0.2084 0.2771 -0.0508 0.0365  -0.0418 19  LYS   B CG  
4239 C  CD  . LYS   B 19  ? 0.3005 0.2381 0.2843 -0.0568 0.0495  -0.0435 19  LYS   B CD  
4240 C  CE  . LYS   B 19  ? 0.3240 0.2629 0.3002 -0.0574 0.0470  -0.0470 19  LYS   B CE  
4241 N  NZ  . LYS   B 19  ? 0.3364 0.2781 0.2977 -0.0611 0.0527  -0.0406 19  LYS   B NZ  
4255 N  N   . ASN   B 20  ? 0.2020 0.1778 0.2804 -0.0215 0.0389  -0.0664 20  ASN   B N   
4256 C  CA  . ASN   B 20  ? 0.2028 0.1910 0.3095 -0.0178 0.0455  -0.0843 20  ASN   B CA  
4257 C  C   . ASN   B 20  ? 0.1979 0.2052 0.3088 -0.0229 0.0607  -0.0994 20  ASN   B C   
4258 O  O   . ASN   B 20  ? 0.2153 0.2429 0.3315 -0.0414 0.0578  -0.1011 20  ASN   B O   
4259 C  CB  . ASN   B 20  ? 0.2318 0.1971 0.3430 0.0062  0.0352  -0.0867 20  ASN   B CB  
4260 C  CG  . ASN   B 20  ? 0.2616 0.2056 0.3620 0.0344  0.0351  -0.1008 20  ASN   B CG  
4261 O  OD1 . ASN   B 20  ? 0.2975 0.2318 0.3853 0.0446  0.0335  -0.1007 20  ASN   B OD1 
4262 N  ND2 . ASN   B 20  ? 0.2521 0.2066 0.3594 0.0371  0.0228  -0.0959 20  ASN   B ND2 
4269 N  N   . ALA   B 21  ? 0.1984 0.1884 0.3040 -0.0288 0.0629  -0.0728 21  ALA   B N   
4270 C  CA  . ALA   B 21  ? 0.2118 0.1929 0.3117 -0.0345 0.0480  -0.0606 21  ALA   B CA  
4271 C  C   . ALA   B 21  ? 0.2119 0.1708 0.2939 -0.0256 0.0465  -0.0453 21  ALA   B C   
4272 O  O   . ALA   B 21  ? 0.2165 0.1645 0.2904 -0.0342 0.0407  -0.0388 21  ALA   B O   
4273 C  CB  . ALA   B 21  ? 0.2297 0.2214 0.3238 -0.0400 0.0528  -0.0395 21  ALA   B CB  
4279 N  N   . ASP   B 22  ? 0.2000 0.1621 0.2903 -0.0223 0.0367  -0.0351 22  ASP   B N   
4280 C  CA  . ASP   B 22  ? 0.1933 0.1543 0.2736 -0.0076 0.0242  -0.0248 22  ASP   B CA  
4281 C  C   . ASP   B 22  ? 0.1861 0.1484 0.2322 -0.0192 0.0179  -0.0166 22  ASP   B C   
4282 O  O   . ASP   B 22  ? 0.1920 0.1527 0.2329 -0.0142 0.0161  -0.0139 22  ASP   B O   
4283 C  CB  . ASP   B 22  ? 0.1960 0.1682 0.3095 -0.0029 0.0256  -0.0076 22  ASP   B CB  
4284 C  CG  . ASP   B 22  ? 0.1933 0.1879 0.3528 0.0007  0.0097  -0.0089 22  ASP   B CG  
4285 O  OD1 . ASP   B 22  ? 0.2044 0.1793 0.3501 0.0032  -0.0081 -0.0118 22  ASP   B OD1 
4286 O  OD2 . ASP   B 22  ? 0.2004 0.2199 0.4074 0.0110  -0.0062 -0.0233 22  ASP   B OD2 
4291 N  N   . ILE   B 23  ? 0.1840 0.1436 0.2003 -0.0161 0.0096  0.0110  23  ILE   B N   
4292 C  CA  . ILE   B 23  ? 0.1749 0.1430 0.1946 -0.0135 0.0030  0.0051  23  ILE   B CA  
4293 C  C   . ILE   B 23  ? 0.1647 0.1421 0.1906 -0.0069 -0.0105 0.0074  23  ILE   B C   
4294 O  O   . ILE   B 23  ? 0.1551 0.1436 0.1847 -0.0128 -0.0112 0.0101  23  ILE   B O   
4295 C  CB  . ILE   B 23  ? 0.1680 0.1504 0.2095 -0.0209 0.0033  0.0145  23  ILE   B CB  
4296 C  CG1 . ILE   B 23  ? 0.1704 0.1569 0.2263 -0.0170 0.0049  0.0276  23  ILE   B CG1 
4297 C  CG2 . ILE   B 23  ? 0.1779 0.1749 0.2159 -0.0208 0.0023  0.0019  23  ILE   B CG2 
4298 C  CD1 . ILE   B 23  ? 0.1751 0.1704 0.2327 -0.0136 0.0045  0.0254  23  ILE   B CD1 
4310 N  N   . VAL   B 24  ? 0.1669 0.1462 0.1968 -0.0068 -0.0121 0.0055  24  VAL   B N   
4311 C  CA  . VAL   B 24  ? 0.1615 0.1521 0.2219 -0.0074 -0.0157 0.0010  24  VAL   B CA  
4312 C  C   . VAL   B 24  ? 0.1571 0.1530 0.2230 -0.0103 -0.0083 0.0011  24  VAL   B C   
4313 O  O   . VAL   B 24  ? 0.1587 0.1621 0.2366 -0.0120 -0.0103 0.0097  24  VAL   B O   
4314 C  CB  . VAL   B 24  ? 0.1717 0.1729 0.2287 0.0009  -0.0236 0.0037  24  VAL   B CB  
4315 C  CG1 . VAL   B 24  ? 0.1688 0.1736 0.2565 -0.0091 -0.0311 0.0031  24  VAL   B CG1 
4316 C  CG2 . VAL   B 24  ? 0.1812 0.2018 0.2280 0.0044  -0.0276 -0.0041 24  VAL   B CG2 
4326 N  N   . GLU   B 25  ? 0.1783 0.1656 0.2269 -0.0075 0.0044  0.0029  25  GLU   B N   
4327 C  CA  . GLU   B 25  ? 0.1911 0.1913 0.2498 0.0013  0.0163  -0.0093 25  GLU   B CA  
4328 C  C   . GLU   B 25  ? 0.1844 0.1842 0.2148 -0.0102 0.0136  0.0030  25  GLU   B C   
4329 O  O   . GLU   B 25  ? 0.1902 0.1990 0.2302 -0.0131 0.0165  0.0089  25  GLU   B O   
4330 C  CB  . GLU   B 25  ? 0.2331 0.2360 0.3167 0.0253  0.0291  -0.0150 25  GLU   B CB  
4331 C  CG  . GLU   B 25  ? 0.2816 0.2938 0.4258 0.0351  0.0255  -0.0138 25  GLU   B CG  
4332 C  CD  . GLU   B 25  ? 0.3152 0.3512 0.5159 0.0336  0.0181  -0.0158 25  GLU   B CD  
4333 O  OE1 . GLU   B 25  ? 0.3479 0.3760 0.5398 0.0399  0.0226  -0.0136 25  GLU   B OE1 
4334 O  OE2 . GLU   B 25  ? 0.3427 0.3706 0.5425 0.0307  0.0090  -0.0230 25  GLU   B OE2 
4341 N  N   . GLU   B 26  ? 0.1817 0.1771 0.1923 -0.0292 0.0112  -0.0027 26  GLU   B N   
4342 C  CA  . GLU   B 26  ? 0.1785 0.1937 0.1987 -0.0413 -0.0077 -0.0008 26  GLU   B CA  
4343 C  C   . GLU   B 26  ? 0.1669 0.1928 0.1876 -0.0279 0.0081  0.0179  26  GLU   B C   
4344 O  O   . GLU   B 26  ? 0.1904 0.2111 0.1959 -0.0248 -0.0002 0.0215  26  GLU   B O   
4345 C  CB  . GLU   B 26  ? 0.2172 0.2113 0.2182 -0.0495 -0.0050 0.0136  26  GLU   B CB  
4346 C  CG  . GLU   B 26  ? 0.2600 0.2505 0.2767 -0.0526 0.0110  -0.0082 26  GLU   B CG  
4347 C  CD  . GLU   B 26  ? 0.2827 0.2760 0.2812 -0.0736 0.0250  -0.0445 26  GLU   B CD  
4348 O  OE1 . GLU   B 26  ? 0.2994 0.2590 0.2895 -0.0827 0.0703  -0.0472 26  GLU   B OE1 
4349 O  OE2 . GLU   B 26  ? 0.2872 0.3165 0.3232 -0.0714 0.0161  -0.0371 26  GLU   B OE2 
4356 N  N   . ALA   B 27  ? 0.1519 0.1747 0.1827 -0.0306 0.0062  0.0201  27  ALA   B N   
4357 C  CA  . ALA   B 27  ? 0.1542 0.1712 0.1974 -0.0203 -0.0006 0.0288  27  ALA   B CA  
4358 C  C   . ALA   B 27  ? 0.1558 0.1793 0.2258 -0.0151 0.0136  0.0396  27  ALA   B C   
4359 O  O   . ALA   B 27  ? 0.1671 0.1885 0.2332 -0.0044 0.0127  0.0442  27  ALA   B O   
4360 C  CB  . ALA   B 27  ? 0.1657 0.1568 0.2003 -0.0197 0.0024  0.0239  27  ALA   B CB  
4366 N  N   . LYS   B 28  ? 0.1524 0.1994 0.2716 -0.0194 0.0180  0.0648  28  LYS   B N   
4367 C  CA  . LYS   B 28  ? 0.1734 0.2395 0.2936 -0.0071 0.0564  0.0953  28  LYS   B CA  
4368 C  C   . LYS   B 28  ? 0.2016 0.2584 0.2788 0.0005  0.0669  0.0829  28  LYS   B C   
4369 O  O   . LYS   B 28  ? 0.2297 0.2632 0.2842 -0.0023 0.0651  0.0775  28  LYS   B O   
4370 C  CB  . LYS   B 28  ? 0.2052 0.2820 0.3541 0.0052  0.0879  0.1173  28  LYS   B CB  
4371 C  CG  . LYS   B 28  ? 0.2467 0.3372 0.3932 0.0063  0.1039  0.1366  28  LYS   B CG  
4372 C  CD  . LYS   B 28  ? 0.3077 0.4070 0.4480 0.0089  0.1191  0.1398  28  LYS   B CD  
4373 C  CE  . LYS   B 28  ? 0.3682 0.4595 0.5039 0.0117  0.1188  0.1427  28  LYS   B CE  
4374 N  NZ  . LYS   B 28  ? 0.4002 0.4870 0.5254 0.0140  0.1144  0.1461  28  LYS   B NZ  
4388 N  N   . LYS   B 29  ? 0.2161 0.2864 0.2820 0.0136  0.0701  0.0712  29  LYS   B N   
4389 C  CA  . LYS   B 29  ? 0.2597 0.3221 0.3056 0.0139  0.0692  0.0726  29  LYS   B CA  
4390 C  C   . LYS   B 29  ? 0.2506 0.3186 0.2635 0.0117  0.0502  0.0812  29  LYS   B C   
4391 O  O   . LYS   B 29  ? 0.2668 0.3367 0.2711 0.0202  0.0494  0.0842  29  LYS   B O   
4392 C  CB  . LYS   B 29  ? 0.3207 0.3646 0.3880 0.0124  0.0702  0.0589  29  LYS   B CB  
4393 C  CG  . LYS   B 29  ? 0.3724 0.3992 0.4804 0.0095  0.0706  0.0507  29  LYS   B CG  
4394 C  CD  . LYS   B 29  ? 0.4192 0.4242 0.5499 0.0048  0.0777  0.0442  29  LYS   B CD  
4395 C  CE  . LYS   B 29  ? 0.4548 0.4433 0.5920 0.0004  0.0860  0.0388  29  LYS   B CE  
4396 N  NZ  . LYS   B 29  ? 0.4733 0.4501 0.6218 -0.0019 0.0885  0.0346  29  LYS   B NZ  
4410 N  N   . VAL   B 30  ? 0.2171 0.2987 0.2431 -0.0054 0.0319  0.0782  30  VAL   B N   
4411 C  CA  . VAL   B 30  ? 0.2054 0.2894 0.2729 -0.0176 -0.0005 0.0752  30  VAL   B CA  
4412 C  C   . VAL   B 30  ? 0.1810 0.2802 0.2652 -0.0183 0.0034  0.0914  30  VAL   B C   
4413 O  O   . VAL   B 30  ? 0.1964 0.2941 0.2786 -0.0118 0.0037  0.1023  30  VAL   B O   
4414 C  CB  . VAL   B 30  ? 0.2109 0.2860 0.3070 -0.0352 -0.0273 0.0712  30  VAL   B CB  
4415 C  CG1 . VAL   B 30  ? 0.2194 0.2930 0.3036 -0.0348 -0.0169 0.0633  30  VAL   B CG1 
4416 C  CG2 . VAL   B 30  ? 0.2221 0.2879 0.3252 -0.0449 -0.0411 0.0636  30  VAL   B CG2 
4426 N  N   . LYS   B 31  ? 0.1713 0.2439 0.2823 -0.0316 -0.0005 0.1010  31  LYS   B N   
4427 C  CA  . LYS   B 31  ? 0.1603 0.2382 0.3175 -0.0391 -0.0046 0.0978  31  LYS   B CA  
4428 C  C   . LYS   B 31  ? 0.1592 0.1995 0.2789 -0.0357 -0.0264 0.0825  31  LYS   B C   
4429 O  O   . LYS   B 31  ? 0.1656 0.2095 0.2900 -0.0321 -0.0224 0.0945  31  LYS   B O   
4430 C  CB  . LYS   B 31  ? 0.1773 0.2852 0.3688 -0.0342 0.0236  0.1122  31  LYS   B CB  
4431 C  CG  . LYS   B 31  ? 0.2115 0.3336 0.4127 -0.0326 0.0367  0.1032  31  LYS   B CG  
4432 C  CD  . LYS   B 31  ? 0.2560 0.3849 0.4595 -0.0299 0.0336  0.0879  31  LYS   B CD  
4433 C  CE  . LYS   B 31  ? 0.2957 0.4139 0.5035 -0.0283 0.0230  0.0759  31  LYS   B CE  
4434 N  NZ  . LYS   B 31  ? 0.3161 0.4377 0.5149 -0.0209 0.0099  0.0679  31  LYS   B NZ  
4448 N  N   . PRO   B 32  ? 0.1742 0.1631 0.2145 -0.0345 -0.0430 0.0493  32  PRO   B N   
4449 C  CA  . PRO   B 32  ? 0.1848 0.1563 0.1858 -0.0382 -0.0415 0.0297  32  PRO   B CA  
4450 C  C   . PRO   B 32  ? 0.1927 0.1500 0.1819 -0.0417 -0.0523 0.0364  32  PRO   B C   
4451 O  O   . PRO   B 32  ? 0.2050 0.1546 0.2180 -0.0478 -0.0688 0.0315  32  PRO   B O   
4452 C  CB  . PRO   B 32  ? 0.2020 0.1500 0.1803 -0.0472 -0.0367 0.0218  32  PRO   B CB  
4453 C  CG  . PRO   B 32  ? 0.2170 0.1437 0.1770 -0.0343 -0.0495 0.0259  32  PRO   B CG  
4454 C  CD  . PRO   B 32  ? 0.2009 0.1470 0.2027 -0.0286 -0.0573 0.0272  32  PRO   B CD  
4462 N  N   . THR   B 33  ? 0.1953 0.1378 0.1766 -0.0369 -0.0497 0.0233  33  THR   B N   
4463 C  CA  . THR   B 33  ? 0.2008 0.1472 0.1709 -0.0411 -0.0464 0.0261  33  THR   B CA  
4464 C  C   . THR   B 33  ? 0.2059 0.1350 0.1700 -0.0428 -0.0458 0.0178  33  THR   B C   
4465 O  O   . THR   B 33  ? 0.2291 0.1385 0.1864 -0.0502 -0.0518 0.0162  33  THR   B O   
4466 C  CB  . THR   B 33  ? 0.2081 0.1601 0.1803 -0.0255 -0.0521 0.0238  33  THR   B CB  
4467 O  OG1 . THR   B 33  ? 0.1977 0.1595 0.1863 -0.0211 -0.0496 0.0252  33  THR   B OG1 
4468 C  CG2 . THR   B 33  ? 0.2309 0.1646 0.2014 -0.0187 -0.0512 0.0259  33  THR   B CG2 
4476 N  N   . VAL   B 34  ? 0.1842 0.1315 0.1598 -0.0399 -0.0428 0.0140  34  VAL   B N   
4477 C  CA  . VAL   B 34  ? 0.1717 0.1312 0.1597 -0.0318 -0.0359 0.0071  34  VAL   B CA  
4478 C  C   . VAL   B 34  ? 0.1569 0.1272 0.1481 -0.0308 -0.0205 0.0091  34  VAL   B C   
4479 O  O   . VAL   B 34  ? 0.1749 0.1301 0.1528 -0.0234 -0.0327 0.0044  34  VAL   B O   
4480 C  CB  . VAL   B 34  ? 0.1779 0.1378 0.1885 -0.0156 -0.0352 0.0068  34  VAL   B CB  
4481 C  CG1 . VAL   B 34  ? 0.1686 0.1556 0.1907 -0.0123 -0.0136 0.0053  34  VAL   B CG1 
4482 C  CG2 . VAL   B 34  ? 0.1839 0.1417 0.2218 -0.0123 -0.0310 0.0106  34  VAL   B CG2 
4492 N  N   . VAL   B 35  ? 0.1459 0.1241 0.1381 -0.0255 -0.0117 0.0089  35  VAL   B N   
4493 C  CA  . VAL   B 35  ? 0.1398 0.1250 0.1403 -0.0220 -0.0081 0.0056  35  VAL   B CA  
4494 C  C   . VAL   B 35  ? 0.1344 0.1169 0.1351 -0.0172 -0.0117 0.0032  35  VAL   B C   
4495 O  O   . VAL   B 35  ? 0.1372 0.1233 0.1464 -0.0232 -0.0000 -0.0024 35  VAL   B O   
4496 C  CB  . VAL   B 35  ? 0.1429 0.1441 0.1483 -0.0177 -0.0016 0.0007  35  VAL   B CB  
4497 C  CG1 . VAL   B 35  ? 0.1364 0.1570 0.1629 -0.0205 -0.0009 0.0002  35  VAL   B CG1 
4498 C  CG2 . VAL   B 35  ? 0.1429 0.1436 0.1562 -0.0101 -0.0050 -0.0030 35  VAL   B CG2 
4508 N  N   . VAL   B 36  ? 0.1349 0.1195 0.1303 -0.0177 -0.0141 0.0094  36  VAL   B N   
4509 C  CA  . VAL   B 36  ? 0.1294 0.1154 0.1316 -0.0155 -0.0124 0.0062  36  VAL   B CA  
4510 C  C   . VAL   B 36  ? 0.1277 0.1183 0.1193 -0.0128 -0.0063 0.0037  36  VAL   B C   
4511 O  O   . VAL   B 36  ? 0.1342 0.1295 0.1548 -0.0126 -0.0038 -0.0016 36  VAL   B O   
4512 C  CB  . VAL   B 36  ? 0.1327 0.1218 0.1392 -0.0160 -0.0070 0.0076  36  VAL   B CB  
4513 C  CG1 . VAL   B 36  ? 0.1305 0.1368 0.1578 -0.0176 -0.0126 0.0022  36  VAL   B CG1 
4514 C  CG2 . VAL   B 36  ? 0.1350 0.1320 0.1499 -0.0130 -0.0128 0.0050  36  VAL   B CG2 
4524 N  N   . ASN   B 37  ? 0.1270 0.1221 0.1310 -0.0037 -0.0073 0.0049  37  ASN   B N   
4525 C  CA  . ASN   B 37  ? 0.1324 0.1272 0.1364 -0.0016 -0.0128 0.0058  37  ASN   B CA  
4526 C  C   . ASN   B 37  ? 0.1307 0.1296 0.1446 0.0025  -0.0090 0.0040  37  ASN   B C   
4527 O  O   . ASN   B 37  ? 0.1375 0.1361 0.1528 -0.0010 -0.0042 0.0073  37  ASN   B O   
4528 C  CB  . ASN   B 37  ? 0.1316 0.1327 0.1310 -0.0058 -0.0123 0.0056  37  ASN   B CB  
4529 C  CG  . ASN   B 37  ? 0.1391 0.1295 0.1493 -0.0055 -0.0115 0.0034  37  ASN   B CG  
4530 O  OD1 . ASN   B 37  ? 0.1457 0.1318 0.1692 0.0061  -0.0156 0.0018  37  ASN   B OD1 
4531 N  ND2 . ASN   B 37  ? 0.1413 0.1256 0.1549 -0.0009 -0.0205 0.0088  37  ASN   B ND2 
4538 N  N   . ALA   B 38  ? 0.1410 0.1239 0.1512 0.0031  0.0033  0.0072  38  ALA   B N   
4539 C  CA  . ALA   B 38  ? 0.1538 0.1326 0.1468 -0.0041 -0.0002 0.0139  38  ALA   B CA  
4540 C  C   . ALA   B 38  ? 0.1468 0.1285 0.1477 -0.0027 0.0001  0.0167  38  ALA   B C   
4541 O  O   . ALA   B 38  ? 0.1580 0.1363 0.1609 0.0034  -0.0050 0.0123  38  ALA   B O   
4542 C  CB  . ALA   B 38  ? 0.1777 0.1362 0.1651 -0.0087 0.0095  0.0010  38  ALA   B CB  
4548 N  N   . ALA   B 39  ? 0.1438 0.1271 0.1400 0.0028  -0.0057 0.0064  39  ALA   B N   
4549 C  CA  . ALA   B 39  ? 0.1535 0.1360 0.1398 0.0037  -0.0077 0.0051  39  ALA   B CA  
4550 C  C   . ALA   B 39  ? 0.1613 0.1410 0.1266 0.0110  -0.0054 0.0065  39  ALA   B C   
4551 O  O   . ALA   B 39  ? 0.1648 0.1483 0.1566 -0.0006 -0.0099 0.0138  39  ALA   B O   
4552 C  CB  . ALA   B 39  ? 0.1533 0.1344 0.1625 -0.0045 -0.0069 0.0003  39  ALA   B CB  
4558 N  N   . ASN   B 40  ? 0.1640 0.1574 0.1316 0.0018  -0.0044 -0.0024 40  ASN   B N   
4559 C  CA  . ASN   B 40  ? 0.1701 0.1663 0.1448 0.0015  -0.0114 -0.0057 40  ASN   B CA  
4560 C  C   . ASN   B 40  ? 0.1766 0.1654 0.1288 0.0112  -0.0088 0.0038  40  ASN   B C   
4561 O  O   . ASN   B 40  ? 0.1705 0.1563 0.1432 0.0133  -0.0110 0.0006  40  ASN   B O   
4562 C  CB  . ASN   B 40  ? 0.1819 0.1670 0.1749 0.0124  -0.0138 0.0151  40  ASN   B CB  
4563 C  CG  . ASN   B 40  ? 0.1859 0.1725 0.2041 0.0077  -0.0251 0.0178  40  ASN   B CG  
4564 O  OD1 . ASN   B 40  ? 0.1837 0.1689 0.2774 0.0082  -0.0383 0.0194  40  ASN   B OD1 
4565 N  ND2 . ASN   B 40  ? 0.1907 0.1705 0.1906 0.0018  -0.0229 0.0185  40  ASN   B ND2 
4572 N  N   . VAL   B 41  ? 0.1798 0.1667 0.1376 0.0163  0.0007  -0.0009 41  VAL   B N   
4573 C  CA  . VAL   B 41  ? 0.1875 0.1804 0.1423 0.0087  0.0053  -0.0037 41  VAL   B CA  
4574 C  C   . VAL   B 41  ? 0.1859 0.1788 0.1365 0.0147  -0.0031 -0.0027 41  VAL   B C   
4575 O  O   . VAL   B 41  ? 0.1841 0.1771 0.1528 0.0124  -0.0094 -0.0057 41  VAL   B O   
4576 C  CB  . VAL   B 41  ? 0.2054 0.1986 0.1743 -0.0063 0.0263  -0.0184 41  VAL   B CB  
4577 C  CG1 . VAL   B 41  ? 0.2035 0.1978 0.1942 -0.0075 0.0399  -0.0200 41  VAL   B CG1 
4578 C  CG2 . VAL   B 41  ? 0.2217 0.2218 0.1843 -0.0148 0.0258  -0.0196 41  VAL   B CG2 
4588 N  N   . TYR   B 42  ? 0.1912 0.1794 0.1456 0.0157  -0.0135 0.0041  42  TYR   B N   
4589 C  CA  . TYR   B 42  ? 0.1973 0.1850 0.1443 0.0151  -0.0176 -0.0116 42  TYR   B CA  
4590 C  C   . TYR   B 42  ? 0.1810 0.1647 0.1550 0.0226  -0.0164 -0.0064 42  TYR   B C   
4591 O  O   . TYR   B 42  ? 0.1845 0.1735 0.1919 0.0145  -0.0272 -0.0157 42  TYR   B O   
4592 C  CB  . TYR   B 42  ? 0.2221 0.2131 0.1537 0.0088  -0.0272 0.0034  42  TYR   B CB  
4593 C  CG  . TYR   B 42  ? 0.2193 0.2293 0.1515 -0.0049 -0.0266 0.0127  42  TYR   B CG  
4594 C  CD1 . TYR   B 42  ? 0.2121 0.2258 0.1240 -0.0095 -0.0089 0.0101  42  TYR   B CD1 
4595 C  CD2 . TYR   B 42  ? 0.2319 0.2395 0.1869 -0.0043 -0.0086 0.0209  42  TYR   B CD2 
4596 C  CE1 . TYR   B 42  ? 0.2248 0.2411 0.1412 -0.0007 -0.0044 0.0128  42  TYR   B CE1 
4597 C  CE2 . TYR   B 42  ? 0.2343 0.2520 0.1881 -0.0015 0.0123  0.0346  42  TYR   B CE2 
4598 C  CZ  . TYR   B 42  ? 0.2451 0.2628 0.1778 0.0161  0.0181  0.0186  42  TYR   B CZ  
4599 O  OH  . TYR   B 42  ? 0.2797 0.2892 0.2197 0.0356  0.0257  0.0269  42  TYR   B OH  
4609 N  N   . LEU   B 43  ? 0.1696 0.1527 0.1465 0.0116  -0.0134 -0.0122 43  LEU   B N   
4610 C  CA  . LEU   B 43  ? 0.1707 0.1526 0.1348 0.0015  -0.0195 -0.0066 43  LEU   B CA  
4611 C  C   . LEU   B 43  ? 0.1729 0.1522 0.1444 0.0039  -0.0150 0.0016  43  LEU   B C   
4612 O  O   . LEU   B 43  ? 0.1681 0.1566 0.1767 0.0080  -0.0175 0.0064  43  LEU   B O   
4613 C  CB  . LEU   B 43  ? 0.1667 0.1470 0.1512 0.0014  -0.0232 -0.0020 43  LEU   B CB  
4614 C  CG  . LEU   B 43  ? 0.1704 0.1468 0.1589 -0.0036 -0.0287 -0.0064 43  LEU   B CG  
4615 C  CD1 . LEU   B 43  ? 0.1753 0.1513 0.1934 -0.0064 -0.0452 -0.0072 43  LEU   B CD1 
4616 C  CD2 . LEU   B 43  ? 0.1663 0.1468 0.1741 -0.0088 -0.0257 -0.0022 43  LEU   B CD2 
4628 N  N   . LYS   B 44  ? 0.1691 0.1523 0.1532 0.0077  -0.0121 -0.0035 44  LYS   B N   
4629 C  CA  . LYS   B 44  ? 0.1821 0.1649 0.1551 0.0116  -0.0148 0.0031  44  LYS   B CA  
4630 C  C   . LYS   B 44  ? 0.1731 0.1570 0.1511 0.0135  -0.0179 -0.0028 44  LYS   B C   
4631 O  O   . LYS   B 44  ? 0.1958 0.1569 0.1810 0.0028  -0.0022 0.0014  44  LYS   B O   
4632 C  CB  . LYS   B 44  ? 0.2115 0.1856 0.1772 0.0208  -0.0329 0.0023  44  LYS   B CB  
4633 C  CG  . LYS   B 44  ? 0.2502 0.2127 0.2206 0.0111  -0.0616 0.0043  44  LYS   B CG  
4634 C  CD  . LYS   B 44  ? 0.2819 0.2328 0.2871 -0.0047 -0.0700 -0.0036 44  LYS   B CD  
4635 C  CE  . LYS   B 44  ? 0.3140 0.2627 0.3384 -0.0119 -0.0731 0.0114  44  LYS   B CE  
4636 N  NZ  . LYS   B 44  ? 0.3246 0.2745 0.3664 -0.0131 -0.0805 0.0311  44  LYS   B NZ  
4650 N  N   . HIS   B 45  ? 0.1624 0.1594 0.1509 0.0098  -0.0155 0.0046  45  HIS   B N   
4651 C  CA  . HIS   B 45  ? 0.1635 0.1526 0.1580 0.0125  -0.0108 0.0020  45  HIS   B CA  
4652 C  C   . HIS   B 45  ? 0.1865 0.1697 0.1934 0.0211  -0.0199 -0.0077 45  HIS   B C   
4653 O  O   . HIS   B 45  ? 0.2025 0.2003 0.2376 0.0409  0.0049  -0.0078 45  HIS   B O   
4654 C  CB  . HIS   B 45  ? 0.1604 0.1606 0.1646 0.0041  -0.0104 0.0011  45  HIS   B CB  
4655 C  CG  . HIS   B 45  ? 0.1572 0.1517 0.1577 -0.0050 -0.0064 -0.0030 45  HIS   B CG  
4656 N  ND1 . HIS   B 45  ? 0.1629 0.1449 0.1613 -0.0030 -0.0120 -0.0082 45  HIS   B ND1 
4657 C  CD2 . HIS   B 45  ? 0.1655 0.1561 0.1694 -0.0125 -0.0132 -0.0024 45  HIS   B CD2 
4658 C  CE1 . HIS   B 45  ? 0.1775 0.1351 0.1488 -0.0061 -0.0208 -0.0109 45  HIS   B CE1 
4659 N  NE2 . HIS   B 45  ? 0.1815 0.1465 0.1554 -0.0048 -0.0180 -0.0021 45  HIS   B NE2 
4667 N  N   . GLY   B 46  ? 0.2022 0.1662 0.2251 0.0168  -0.0442 0.0062  46  GLY   B N   
4668 C  CA  . GLY   B 46  ? 0.2200 0.1808 0.2618 0.0132  -0.0531 0.0090  46  GLY   B CA  
4669 C  C   . GLY   B 46  ? 0.2182 0.2006 0.3052 0.0250  -0.0481 0.0058  46  GLY   B C   
4670 O  O   . GLY   B 46  ? 0.2312 0.2270 0.3963 0.0276  -0.0193 -0.0268 46  GLY   B O   
4674 N  N   . GLY   B 47  ? 0.2096 0.2073 0.2804 0.0072  -0.0228 0.0030  47  GLY   B N   
4675 C  CA  . GLY   B 47  ? 0.1988 0.1831 0.2427 0.0020  -0.0186 0.0066  47  GLY   B CA  
4676 C  C   . GLY   B 47  ? 0.1770 0.1609 0.2073 -0.0007 -0.0063 0.0103  47  GLY   B C   
4677 O  O   . GLY   B 47  ? 0.1859 0.1469 0.2186 0.0043  -0.0112 0.0136  47  GLY   B O   
4681 N  N   . GLY   B 48  ? 0.1631 0.1523 0.2003 -0.0014 -0.0127 0.0227  48  GLY   B N   
4682 C  CA  . GLY   B 48  ? 0.1553 0.1488 0.1984 -0.0079 -0.0070 0.0091  48  GLY   B CA  
4683 C  C   . GLY   B 48  ? 0.1471 0.1474 0.1887 -0.0002 0.0046  0.0072  48  GLY   B C   
4684 O  O   . GLY   B 48  ? 0.1450 0.1516 0.2103 0.0041  -0.0079 0.0023  48  GLY   B O   
4688 N  N   . VAL   B 49  ? 0.1503 0.1503 0.1795 0.0109  -0.0006 0.0080  49  VAL   B N   
4689 C  CA  . VAL   B 49  ? 0.1541 0.1547 0.1689 0.0145  -0.0132 -0.0049 49  VAL   B CA  
4690 C  C   . VAL   B 49  ? 0.1433 0.1441 0.1558 0.0144  -0.0129 0.0030  49  VAL   B C   
4691 O  O   . VAL   B 49  ? 0.1533 0.1507 0.1738 0.0044  0.0003  0.0060  49  VAL   B O   
4692 C  CB  . VAL   B 49  ? 0.1583 0.1744 0.1864 0.0083  -0.0264 -0.0072 49  VAL   B CB  
4693 C  CG1 . VAL   B 49  ? 0.1577 0.1789 0.1832 0.0124  -0.0321 -0.0009 49  VAL   B CG1 
4694 C  CG2 . VAL   B 49  ? 0.1771 0.1914 0.2086 -0.0038 -0.0388 -0.0131 49  VAL   B CG2 
4704 N  N   . ALA   B 50  ? 0.1430 0.1411 0.1613 0.0041  -0.0116 0.0029  50  ALA   B N   
4705 C  CA  . ALA   B 50  ? 0.1447 0.1313 0.1634 0.0074  -0.0073 0.0063  50  ALA   B CA  
4706 C  C   . ALA   B 50  ? 0.1532 0.1356 0.1507 0.0054  -0.0015 -0.0015 50  ALA   B C   
4707 O  O   . ALA   B 50  ? 0.1541 0.1363 0.1602 0.0046  -0.0035 -0.0054 50  ALA   B O   
4708 C  CB  . ALA   B 50  ? 0.1499 0.1372 0.1615 0.0053  -0.0070 0.0045  50  ALA   B CB  
4714 N  N   . GLY   B 51  ? 0.1492 0.1496 0.1651 0.0113  -0.0132 0.0081  51  GLY   B N   
4715 C  CA  . GLY   B 51  ? 0.1416 0.1534 0.1981 0.0227  -0.0205 0.0105  51  GLY   B CA  
4716 C  C   . GLY   B 51  ? 0.1430 0.1526 0.1866 0.0204  -0.0093 0.0042  51  GLY   B C   
4717 O  O   . GLY   B 51  ? 0.1475 0.1700 0.2022 0.0060  -0.0083 -0.0020 51  GLY   B O   
4721 N  N   . ALA   B 52  ? 0.1451 0.1525 0.1789 0.0181  -0.0075 0.0075  52  ALA   B N   
4722 C  CA  . ALA   B 52  ? 0.1543 0.1571 0.1843 0.0151  -0.0013 -0.0085 52  ALA   B CA  
4723 C  C   . ALA   B 52  ? 0.1406 0.1526 0.1676 0.0092  0.0011  -0.0007 52  ALA   B C   
4724 O  O   . ALA   B 52  ? 0.1427 0.1589 0.1880 0.0096  0.0043  -0.0016 52  ALA   B O   
4725 C  CB  . ALA   B 52  ? 0.1702 0.1593 0.1834 0.0059  0.0096  -0.0069 52  ALA   B CB  
4731 N  N   . LEU   B 53  ? 0.1352 0.1483 0.1559 0.0168  -0.0033 0.0010  53  LEU   B N   
4732 C  CA  . LEU   B 53  ? 0.1383 0.1564 0.1536 0.0085  -0.0085 0.0012  53  LEU   B CA  
4733 C  C   . LEU   B 53  ? 0.1455 0.1510 0.1473 0.0103  0.0039  0.0046  53  LEU   B C   
4734 O  O   . LEU   B 53  ? 0.1509 0.1573 0.1735 0.0037  -0.0022 0.0099  53  LEU   B O   
4735 C  CB  . LEU   B 53  ? 0.1357 0.1639 0.1762 0.0061  -0.0004 0.0118  53  LEU   B CB  
4736 C  CG  . LEU   B 53  ? 0.1385 0.1715 0.1770 0.0009  -0.0001 0.0177  53  LEU   B CG  
4737 C  CD1 . LEU   B 53  ? 0.1457 0.1914 0.2000 0.0128  -0.0011 0.0010  53  LEU   B CD1 
4738 C  CD2 . LEU   B 53  ? 0.1551 0.2029 0.1994 -0.0095 -0.0141 -0.0083 53  LEU   B CD2 
4750 N  N   . ASN   B 54  ? 0.1454 0.1373 0.1464 0.0064  -0.0051 0.0012  54  ASN   B N   
4751 C  CA  . ASN   B 54  ? 0.1519 0.1510 0.1627 0.0017  -0.0040 -0.0043 54  ASN   B CA  
4752 C  C   . ASN   B 54  ? 0.1435 0.1552 0.1813 0.0030  0.0047  -0.0040 54  ASN   B C   
4753 O  O   . ASN   B 54  ? 0.1404 0.1640 0.1937 -0.0020 0.0003  -0.0055 54  ASN   B O   
4754 C  CB  . ASN   B 54  ? 0.1514 0.1641 0.1767 0.0047  0.0020  -0.0006 54  ASN   B CB  
4755 C  CG  . ASN   B 54  ? 0.1499 0.1694 0.1824 0.0021  -0.0113 0.0009  54  ASN   B CG  
4756 O  OD1 . ASN   B 54  ? 0.1484 0.1677 0.1905 -0.0047 -0.0124 -0.0128 54  ASN   B OD1 
4757 N  ND2 . ASN   B 54  ? 0.1632 0.1885 0.2057 -0.0011 -0.0383 0.0064  54  ASN   B ND2 
4764 N  N   . LYS   B 55  ? 0.1381 0.1596 0.2050 0.0079  -0.0039 -0.0016 55  LYS   B N   
4765 C  CA  . LYS   B 55  ? 0.1456 0.1694 0.2202 0.0142  -0.0034 -0.0020 55  LYS   B CA  
4766 C  C   . LYS   B 55  ? 0.1425 0.1683 0.2156 0.0130  0.0062  -0.0073 55  LYS   B C   
4767 O  O   . LYS   B 55  ? 0.1393 0.1848 0.2365 0.0102  0.0074  -0.0069 55  LYS   B O   
4768 C  CB  . LYS   B 55  ? 0.1583 0.1841 0.2664 0.0235  0.0032  0.0022  55  LYS   B CB  
4769 C  CG  . LYS   B 55  ? 0.2019 0.2125 0.3478 0.0309  0.0135  0.0264  55  LYS   B CG  
4770 C  CD  . LYS   B 55  ? 0.2423 0.2373 0.4149 0.0358  0.0319  0.0456  55  LYS   B CD  
4771 C  CE  . LYS   B 55  ? 0.2667 0.2603 0.4828 0.0335  0.0498  0.0499  55  LYS   B CE  
4772 N  NZ  . LYS   B 55  ? 0.2731 0.2750 0.5177 0.0313  0.0387  0.0582  55  LYS   B NZ  
4786 N  N   . ALA   B 56  ? 0.1408 0.1748 0.1984 0.0092  0.0021  -0.0059 56  ALA   B N   
4787 C  CA  . ALA   B 56  ? 0.1576 0.1928 0.1984 0.0030  0.0058  -0.0047 56  ALA   B CA  
4788 C  C   . ALA   B 56  ? 0.1568 0.1892 0.1917 0.0016  0.0131  -0.0005 56  ALA   B C   
4789 O  O   . ALA   B 56  ? 0.1686 0.2001 0.2103 0.0075  0.0280  -0.0022 56  ALA   B O   
4790 C  CB  . ALA   B 56  ? 0.1693 0.2128 0.2102 -0.0118 0.0018  -0.0114 56  ALA   B CB  
4796 N  N   . THR   B 57  ? 0.1495 0.1768 0.1991 -0.0006 0.0171  0.0004  57  THR   B N   
4797 C  CA  . THR   B 57  ? 0.1545 0.1771 0.1980 -0.0024 0.0220  0.0050  57  THR   B CA  
4798 C  C   . THR   B 57  ? 0.1565 0.1801 0.2136 0.0002  0.0220  0.0090  57  THR   B C   
4799 O  O   . THR   B 57  ? 0.1678 0.1808 0.2234 -0.0162 0.0177  0.0039  57  THR   B O   
4800 C  CB  . THR   B 57  ? 0.1626 0.1626 0.1733 -0.0013 0.0149  0.0125  57  THR   B CB  
4801 O  OG1 . THR   B 57  ? 0.1615 0.1573 0.1997 -0.0059 0.0120  0.0009  57  THR   B OG1 
4802 C  CG2 . THR   B 57  ? 0.1600 0.1690 0.1694 0.0003  0.0166  0.0100  57  THR   B CG2 
4810 N  N   . ASN   B 58  ? 0.1406 0.1991 0.2434 -0.0100 0.0029  -0.0078 58  ASN   B N   
4811 C  CA  . ASN   B 58  ? 0.1613 0.2445 0.2869 -0.0251 0.0281  -0.0007 58  ASN   B CA  
4812 C  C   . ASN   B 58  ? 0.1455 0.2226 0.2450 -0.0161 0.0023  -0.0043 58  ASN   B C   
4813 O  O   . ASN   B 58  ? 0.1525 0.2365 0.2535 -0.0183 -0.0004 -0.0161 58  ASN   B O   
4814 C  CB  . ASN   B 58  ? 0.2579 0.3225 0.4096 -0.0403 0.0688  0.0148  58  ASN   B CB  
4815 C  CG  . ASN   B 58  ? 0.3809 0.4092 0.5473 -0.0438 0.0935  0.0370  58  ASN   B CG  
4816 O  OD1 . ASN   B 58  ? 0.4000 0.4206 0.5988 -0.0455 0.0996  0.0429  58  ASN   B OD1 
4817 N  ND2 . ASN   B 58  ? 0.4526 0.4526 0.5938 -0.0453 0.1046  0.0414  58  ASN   B ND2 
4824 N  N   . ASN   B 59  ? 0.1492 0.2079 0.2300 -0.0103 -0.0002 0.0020  59  ASN   B N   
4825 C  CA  . ASN   B 59  ? 0.1544 0.2079 0.2137 -0.0094 -0.0192 0.0100  59  ASN   B CA  
4826 C  C   . ASN   B 59  ? 0.1454 0.1979 0.1972 -0.0119 -0.0216 -0.0038 59  ASN   B C   
4827 O  O   . ASN   B 59  ? 0.1513 0.2017 0.1921 -0.0129 -0.0093 -0.0052 59  ASN   B O   
4828 C  CB  . ASN   B 59  ? 0.1667 0.2272 0.2245 -0.0050 -0.0262 0.0160  59  ASN   B CB  
4829 C  CG  . ASN   B 59  ? 0.1726 0.2380 0.2383 -0.0058 -0.0426 0.0103  59  ASN   B CG  
4830 O  OD1 . ASN   B 59  ? 0.1757 0.2406 0.2385 -0.0042 -0.0263 0.0272  59  ASN   B OD1 
4831 N  ND2 . ASN   B 59  ? 0.1773 0.2481 0.2441 -0.0102 -0.0459 -0.0008 59  ASN   B ND2 
4838 N  N   . ALA   B 60  ? 0.1420 0.1854 0.2017 -0.0136 -0.0067 -0.0028 60  ALA   B N   
4839 C  CA  . ALA   B 60  ? 0.1531 0.1745 0.2072 -0.0156 -0.0065 0.0024  60  ALA   B CA  
4840 C  C   . ALA   B 60  ? 0.1615 0.1594 0.1896 -0.0131 -0.0072 0.0019  60  ALA   B C   
4841 O  O   . ALA   B 60  ? 0.1640 0.1617 0.1982 -0.0182 -0.0034 -0.0091 60  ALA   B O   
4842 C  CB  . ALA   B 60  ? 0.1675 0.1738 0.2271 -0.0175 0.0028  0.0004  60  ALA   B CB  
4848 N  N   . MET   B 61  ? 0.1553 0.1499 0.1748 -0.0153 -0.0026 0.0072  61  MET   B N   
4849 C  CA  . MET   B 61  ? 0.1460 0.1491 0.1714 -0.0097 -0.0100 0.0067  61  MET   B CA  
4850 C  C   . MET   B 61  ? 0.1532 0.1483 0.1722 -0.0150 -0.0101 0.0048  61  MET   B C   
4851 O  O   . MET   B 61  ? 0.1565 0.1463 0.1648 -0.0022 -0.0058 -0.0150 61  MET   B O   
4852 C  CB  . MET   B 61  ? 0.1397 0.1503 0.1706 -0.0038 -0.0101 -0.0041 61  MET   B CB  
4853 C  CG  . MET   B 61  ? 0.1403 0.1497 0.1670 0.0022  -0.0130 0.0071  61  MET   B CG  
4854 S  SD  . MET   B 61  ? 0.1424 0.1508 0.1851 -0.0030 -0.0083 -0.0082 61  MET   B SD  
4855 C  CE  . MET   B 61  ? 0.1505 0.1672 0.2073 0.0014  -0.0022 -0.0274 61  MET   B CE  
4865 N  N   . GLN   B 62  ? 0.1487 0.1564 0.1641 -0.0101 -0.0221 0.0028  62  GLN   B N   
4866 C  CA  . GLN   B 62  ? 0.1544 0.1611 0.1730 -0.0016 -0.0215 0.0001  62  GLN   B CA  
4867 C  C   . GLN   B 62  ? 0.1550 0.1648 0.1778 -0.0029 -0.0227 -0.0049 62  GLN   B C   
4868 O  O   . GLN   B 62  ? 0.1678 0.1623 0.1843 -0.0028 -0.0332 -0.0100 62  GLN   B O   
4869 C  CB  . GLN   B 62  ? 0.1586 0.1659 0.1812 0.0025  -0.0204 0.0028  62  GLN   B CB  
4870 C  CG  . GLN   B 62  ? 0.1652 0.1710 0.1747 0.0046  -0.0268 -0.0017 62  GLN   B CG  
4871 C  CD  . GLN   B 62  ? 0.1636 0.1628 0.1702 0.0039  -0.0268 0.0067  62  GLN   B CD  
4872 O  OE1 . GLN   B 62  ? 0.1604 0.1584 0.1905 0.0007  -0.0275 -0.0052 62  GLN   B OE1 
4873 N  NE2 . GLN   B 62  ? 0.1631 0.1696 0.1740 0.0028  -0.0223 -0.0079 62  GLN   B NE2 
4882 N  N   . VAL   B 63  ? 0.1540 0.1679 0.1921 -0.0054 -0.0258 -0.0075 63  VAL   B N   
4883 C  CA  . VAL   B 63  ? 0.1655 0.1705 0.2155 -0.0120 -0.0321 -0.0027 63  VAL   B CA  
4884 C  C   . VAL   B 63  ? 0.1662 0.1582 0.1971 -0.0241 -0.0338 -0.0136 63  VAL   B C   
4885 O  O   . VAL   B 63  ? 0.1755 0.1565 0.2126 -0.0184 -0.0426 -0.0144 63  VAL   B O   
4886 C  CB  . VAL   B 63  ? 0.1606 0.1873 0.2499 -0.0164 -0.0285 -0.0095 63  VAL   B CB  
4887 C  CG1 . VAL   B 63  ? 0.1712 0.1915 0.2619 -0.0271 -0.0147 -0.0043 63  VAL   B CG1 
4888 C  CG2 . VAL   B 63  ? 0.1529 0.2114 0.2520 -0.0121 -0.0370 -0.0159 63  VAL   B CG2 
4898 N  N   . GLU   B 64  ? 0.1609 0.1524 0.1798 -0.0144 -0.0253 -0.0104 64  GLU   B N   
4899 C  CA  . GLU   B 64  ? 0.1650 0.1490 0.1832 -0.0123 -0.0304 0.0008  64  GLU   B CA  
4900 C  C   . GLU   B 64  ? 0.1573 0.1428 0.1778 -0.0070 -0.0279 -0.0099 64  GLU   B C   
4901 O  O   . GLU   B 64  ? 0.1667 0.1504 0.1802 -0.0076 -0.0259 -0.0110 64  GLU   B O   
4902 C  CB  . GLU   B 64  ? 0.1648 0.1566 0.1686 -0.0173 -0.0231 0.0050  64  GLU   B CB  
4903 C  CG  . GLU   B 64  ? 0.1715 0.1641 0.1686 -0.0290 -0.0212 -0.0091 64  GLU   B CG  
4904 C  CD  . GLU   B 64  ? 0.1751 0.1765 0.1824 -0.0305 -0.0272 -0.0065 64  GLU   B CD  
4905 O  OE1 . GLU   B 64  ? 0.1775 0.1903 0.2009 -0.0323 -0.0224 -0.0232 64  GLU   B OE1 
4906 O  OE2 . GLU   B 64  ? 0.1873 0.1863 0.1847 -0.0383 -0.0399 -0.0086 64  GLU   B OE2 
4913 N  N   . SER   B 65  ? 0.1603 0.1412 0.1625 -0.0084 -0.0175 -0.0136 65  SER   B N   
4914 C  CA  . SER   B 65  ? 0.1569 0.1399 0.1693 0.0001  -0.0182 -0.0120 65  SER   B CA  
4915 C  C   . SER   B 65  ? 0.1579 0.1379 0.1636 0.0031  -0.0275 -0.0181 65  SER   B C   
4916 O  O   . SER   B 65  ? 0.1640 0.1550 0.1712 -0.0002 -0.0238 -0.0224 65  SER   B O   
4917 C  CB  . SER   B 65  ? 0.1552 0.1456 0.1755 -0.0098 -0.0180 -0.0102 65  SER   B CB  
4918 O  OG  . SER   B 65  ? 0.1595 0.1468 0.1787 -0.0105 -0.0222 -0.0183 65  SER   B OG  
4924 N  N   . ASP   B 66  ? 0.1690 0.1515 0.1675 -0.0008 -0.0277 -0.0142 66  ASP   B N   
4925 C  CA  . ASP   B 66  ? 0.1804 0.1626 0.1543 -0.0003 -0.0354 -0.0073 66  ASP   B CA  
4926 C  C   . ASP   B 66  ? 0.1831 0.1620 0.1637 -0.0062 -0.0293 -0.0132 66  ASP   B C   
4927 O  O   . ASP   B 66  ? 0.1862 0.1641 0.1731 0.0031  -0.0269 -0.0170 66  ASP   B O   
4928 C  CB  . ASP   B 66  ? 0.1921 0.1743 0.1851 0.0087  -0.0463 -0.0108 66  ASP   B CB  
4929 C  CG  . ASP   B 66  ? 0.2189 0.1906 0.2133 0.0182  -0.0601 -0.0037 66  ASP   B CG  
4930 O  OD1 . ASP   B 66  ? 0.2442 0.1852 0.2169 0.0111  -0.0577 0.0032  66  ASP   B OD1 
4931 O  OD2 . ASP   B 66  ? 0.2349 0.2129 0.2759 0.0345  -0.0554 -0.0021 66  ASP   B OD2 
4936 N  N   . ASP   B 67  ? 0.1722 0.1568 0.1581 -0.0098 -0.0262 -0.0197 67  ASP   B N   
4937 C  CA  . ASP   B 67  ? 0.1886 0.1462 0.1768 -0.0041 -0.0224 -0.0064 67  ASP   B CA  
4938 C  C   . ASP   B 67  ? 0.1834 0.1526 0.1903 0.0021  -0.0269 -0.0199 67  ASP   B C   
4939 O  O   . ASP   B 67  ? 0.1862 0.1597 0.1975 0.0001  -0.0158 -0.0219 67  ASP   B O   
4940 C  CB  . ASP   B 67  ? 0.2161 0.1583 0.1918 -0.0137 -0.0349 -0.0099 67  ASP   B CB  
4941 C  CG  . ASP   B 67  ? 0.2543 0.1670 0.2118 -0.0139 -0.0561 -0.0122 67  ASP   B CG  
4942 O  OD1 . ASP   B 67  ? 0.2751 0.1724 0.2261 -0.0149 -0.0616 -0.0067 67  ASP   B OD1 
4943 O  OD2 . ASP   B 67  ? 0.2662 0.1740 0.2342 0.0006  -0.0684 -0.0061 67  ASP   B OD2 
4948 N  N   . TYR   B 68  ? 0.1771 0.1523 0.1807 0.0048  -0.0361 -0.0226 68  TYR   B N   
4949 C  CA  . TYR   B 68  ? 0.1724 0.1652 0.1932 0.0103  -0.0365 -0.0278 68  TYR   B CA  
4950 C  C   . TYR   B 68  ? 0.1684 0.1659 0.1771 0.0055  -0.0331 -0.0371 68  TYR   B C   
4951 O  O   . TYR   B 68  ? 0.1777 0.1760 0.1993 0.0089  -0.0285 -0.0474 68  TYR   B O   
4952 C  CB  . TYR   B 68  ? 0.1746 0.1823 0.2000 0.0111  -0.0413 -0.0370 68  TYR   B CB  
4953 C  CG  . TYR   B 68  ? 0.1889 0.1974 0.2072 0.0131  -0.0350 -0.0543 68  TYR   B CG  
4954 C  CD1 . TYR   B 68  ? 0.1944 0.2038 0.2321 -0.0040 -0.0309 -0.0538 68  TYR   B CD1 
4955 C  CD2 . TYR   B 68  ? 0.1975 0.2195 0.2240 0.0195  -0.0501 -0.0500 68  TYR   B CD2 
4956 C  CE1 . TYR   B 68  ? 0.1996 0.2202 0.2525 -0.0001 -0.0356 -0.0549 68  TYR   B CE1 
4957 C  CE2 . TYR   B 68  ? 0.2005 0.2283 0.2352 0.0204  -0.0439 -0.0643 68  TYR   B CE2 
4958 C  CZ  . TYR   B 68  ? 0.1955 0.2302 0.2558 0.0107  -0.0410 -0.0655 68  TYR   B CZ  
4959 O  OH  . TYR   B 68  ? 0.1845 0.2488 0.2913 0.0115  -0.0378 -0.0493 68  TYR   B OH  
4969 N  N   . ILE   B 69  ? 0.1666 0.1555 0.1828 0.0030  -0.0299 -0.0323 69  ILE   B N   
4970 C  CA  . ILE   B 69  ? 0.1790 0.1615 0.1894 0.0002  -0.0217 -0.0366 69  ILE   B CA  
4971 C  C   . ILE   B 69  ? 0.1785 0.1603 0.1876 0.0087  -0.0311 -0.0296 69  ILE   B C   
4972 O  O   . ILE   B 69  ? 0.1826 0.1677 0.1838 0.0062  -0.0180 -0.0280 69  ILE   B O   
4973 C  CB  . ILE   B 69  ? 0.1892 0.1629 0.2096 0.0003  -0.0019 -0.0298 69  ILE   B CB  
4974 C  CG1 . ILE   B 69  ? 0.1878 0.1645 0.2143 -0.0046 0.0056  -0.0246 69  ILE   B CG1 
4975 C  CG2 . ILE   B 69  ? 0.2056 0.1727 0.2209 -0.0005 0.0049  -0.0228 69  ILE   B CG2 
4976 C  CD1 . ILE   B 69  ? 0.1833 0.1754 0.2248 -0.0106 0.0094  -0.0202 69  ILE   B CD1 
4988 N  N   . ALA   B 70  ? 0.1760 0.1589 0.1941 0.0081  -0.0390 -0.0212 70  ALA   B N   
4989 C  CA  . ALA   B 70  ? 0.1781 0.1618 0.1716 0.0050  -0.0403 -0.0218 70  ALA   B CA  
4990 C  C   . ALA   B 70  ? 0.1903 0.1642 0.1798 -0.0005 -0.0382 -0.0308 70  ALA   B C   
4991 O  O   . ALA   B 70  ? 0.1925 0.1669 0.1899 0.0018  -0.0376 -0.0306 70  ALA   B O   
4992 C  CB  . ALA   B 70  ? 0.1790 0.1798 0.1744 -0.0030 -0.0359 -0.0254 70  ALA   B CB  
4998 N  N   . THR   B 71  ? 0.1982 0.1640 0.1865 0.0045  -0.0494 -0.0326 71  THR   B N   
4999 C  CA  . THR   B 71  ? 0.2066 0.1697 0.2071 0.0104  -0.0619 -0.0360 71  THR   B CA  
5000 C  C   . THR   B 71  ? 0.2015 0.1752 0.2402 0.0261  -0.0609 -0.0475 71  THR   B C   
5001 O  O   . THR   B 71  ? 0.2097 0.1773 0.2784 0.0295  -0.0539 -0.0572 71  THR   B O   
5002 C  CB  . THR   B 71  ? 0.2283 0.1898 0.2342 0.0028  -0.0736 -0.0112 71  THR   B CB  
5003 O  OG1 . THR   B 71  ? 0.2430 0.2170 0.2817 -0.0217 -0.0730 0.0097  71  THR   B OG1 
5004 C  CG2 . THR   B 71  ? 0.2464 0.1876 0.2565 0.0090  -0.0617 -0.0035 71  THR   B CG2 
5012 N  N   . ASN   B 72  ? 0.1850 0.1783 0.2336 0.0201  -0.0593 -0.0661 72  ASN   B N   
5013 C  CA  . ASN   B 72  ? 0.1846 0.1935 0.2302 0.0173  -0.0466 -0.0737 72  ASN   B CA  
5014 C  C   . ASN   B 72  ? 0.1880 0.2071 0.2355 0.0041  -0.0267 -0.0679 72  ASN   B C   
5015 O  O   . ASN   B 72  ? 0.1868 0.2239 0.2663 0.0071  -0.0111 -0.0715 72  ASN   B O   
5016 C  CB  . ASN   B 72  ? 0.1931 0.2087 0.2352 0.0153  -0.0535 -0.0613 72  ASN   B CB  
5017 C  CG  . ASN   B 72  ? 0.2087 0.2212 0.2374 0.0354  -0.0585 -0.0409 72  ASN   B CG  
5018 O  OD1 . ASN   B 72  ? 0.2328 0.2412 0.2413 0.0209  -0.0379 -0.0417 72  ASN   B OD1 
5019 N  ND2 . ASN   B 72  ? 0.2240 0.2315 0.2797 0.0489  -0.0516 -0.0078 72  ASN   B ND2 
5026 N  N   . GLY   B 73  ? 0.1894 0.2032 0.2168 -0.0024 -0.0325 -0.0586 73  GLY   B N   
5027 C  CA  . GLY   B 73  ? 0.1837 0.2097 0.1947 -0.0040 -0.0213 -0.0493 73  GLY   B CA  
5028 C  C   . GLY   B 73  ? 0.1814 0.2058 0.1528 0.0098  -0.0286 -0.0441 73  GLY   B C   
5029 O  O   . GLY   B 73  ? 0.1716 0.1944 0.1724 0.0098  -0.0209 -0.0322 73  GLY   B O   
5033 N  N   . PRO   B 74  ? 0.1831 0.2133 0.1520 0.0086  -0.0273 -0.0341 74  PRO   B N   
5034 C  CA  . PRO   B 74  ? 0.1756 0.2139 0.1413 0.0139  -0.0186 -0.0244 74  PRO   B CA  
5035 C  C   . PRO   B 74  ? 0.1612 0.1953 0.1565 0.0111  -0.0132 -0.0163 74  PRO   B C   
5036 O  O   . PRO   B 74  ? 0.1695 0.1949 0.1993 0.0122  -0.0102 -0.0235 74  PRO   B O   
5037 C  CB  . PRO   B 74  ? 0.1882 0.2345 0.1476 0.0039  -0.0137 -0.0202 74  PRO   B CB  
5038 C  CG  . PRO   B 74  ? 0.2046 0.2422 0.1720 0.0015  -0.0158 -0.0170 74  PRO   B CG  
5039 C  CD  . PRO   B 74  ? 0.2056 0.2321 0.1670 0.0074  -0.0162 -0.0265 74  PRO   B CD  
5047 N  N   . LEU   B 75  ? 0.1609 0.1834 0.1441 0.0114  -0.0163 -0.0153 75  LEU   B N   
5048 C  CA  . LEU   B 75  ? 0.1647 0.1861 0.1404 0.0056  -0.0170 0.0025  75  LEU   B CA  
5049 C  C   . LEU   B 75  ? 0.1714 0.1992 0.1329 0.0098  -0.0044 0.0002  75  LEU   B C   
5050 O  O   . LEU   B 75  ? 0.1866 0.2118 0.1523 -0.0021 -0.0077 0.0031  75  LEU   B O   
5051 C  CB  . LEU   B 75  ? 0.1755 0.1875 0.1410 -0.0062 -0.0189 0.0147  75  LEU   B CB  
5052 C  CG  . LEU   B 75  ? 0.2105 0.2027 0.1609 -0.0243 -0.0033 0.0091  75  LEU   B CG  
5053 C  CD1 . LEU   B 75  ? 0.2352 0.2170 0.1622 -0.0325 0.0192  -0.0020 75  LEU   B CD1 
5054 C  CD2 . LEU   B 75  ? 0.2463 0.2228 0.2276 -0.0161 0.0126  0.0183  75  LEU   B CD2 
5066 N  N   . LYS   B 76  ? 0.1693 0.2197 0.1648 0.0095  0.0000  0.0113  76  LYS   B N   
5067 C  CA  . LYS   B 76  ? 0.1824 0.2278 0.1976 -0.0004 0.0214  0.0075  76  LYS   B CA  
5068 C  C   . LYS   B 76  ? 0.1758 0.2132 0.1768 0.0039  0.0170  0.0267  76  LYS   B C   
5069 O  O   . LYS   B 76  ? 0.1767 0.1889 0.1844 -0.0007 0.0115  0.0235  76  LYS   B O   
5070 C  CB  . LYS   B 76  ? 0.2013 0.2315 0.2473 -0.0114 0.0355  -0.0250 76  LYS   B CB  
5071 C  CG  . LYS   B 76  ? 0.2142 0.2513 0.2872 -0.0051 0.0243  -0.0340 76  LYS   B CG  
5072 C  CD  . LYS   B 76  ? 0.2163 0.2616 0.3222 0.0011  0.0161  -0.0457 76  LYS   B CD  
5073 C  CE  . LYS   B 76  ? 0.2187 0.2807 0.3756 0.0001  -0.0002 -0.0522 76  LYS   B CE  
5074 N  NZ  . LYS   B 76  ? 0.2171 0.2866 0.3897 -0.0051 -0.0249 -0.0700 76  LYS   B NZ  
5088 N  N   . VAL   B 77  ? 0.1810 0.2263 0.1772 0.0090  0.0144  0.0294  77  VAL   B N   
5089 C  CA  . VAL   B 77  ? 0.1860 0.2184 0.1898 0.0123  0.0154  0.0528  77  VAL   B CA  
5090 C  C   . VAL   B 77  ? 0.1701 0.1899 0.1810 0.0102  0.0216  0.0380  77  VAL   B C   
5091 O  O   . VAL   B 77  ? 0.1736 0.1843 0.1848 0.0214  0.0266  0.0310  77  VAL   B O   
5092 C  CB  . VAL   B 77  ? 0.1976 0.2269 0.2303 0.0139  0.0271  0.0719  77  VAL   B CB  
5093 C  CG1 . VAL   B 77  ? 0.1988 0.2173 0.2557 0.0104  0.0321  0.0878  77  VAL   B CG1 
5094 C  CG2 . VAL   B 77  ? 0.2130 0.2436 0.2484 0.0107  0.0084  0.0698  77  VAL   B CG2 
5104 N  N   . GLY   B 78  ? 0.1646 0.1786 0.1847 0.0069  0.0137  0.0288  78  GLY   B N   
5105 C  CA  . GLY   B 78  ? 0.1646 0.1698 0.1723 0.0078  0.0219  0.0160  78  GLY   B CA  
5106 C  C   . GLY   B 78  ? 0.1570 0.1587 0.1635 0.0125  0.0168  0.0197  78  GLY   B C   
5107 O  O   . GLY   B 78  ? 0.1607 0.1574 0.1772 0.0157  0.0189  0.0225  78  GLY   B O   
5111 N  N   . GLY   B 79  ? 0.1504 0.1630 0.1717 0.0099  0.0148  0.0152  79  GLY   B N   
5112 C  CA  . GLY   B 79  ? 0.1541 0.1544 0.1696 0.0145  0.0065  0.0114  79  GLY   B CA  
5113 C  C   . GLY   B 79  ? 0.1431 0.1484 0.1602 0.0135  0.0111  0.0094  79  GLY   B C   
5114 O  O   . GLY   B 79  ? 0.1499 0.1463 0.1784 0.0108  0.0168  0.0218  79  GLY   B O   
5118 N  N   . SER   B 80  ? 0.1438 0.1405 0.1753 0.0073  0.0197  0.0097  80  SER   B N   
5119 C  CA  . SER   B 80  ? 0.1369 0.1407 0.1689 0.0053  0.0082  0.0096  80  SER   B CA  
5120 C  C   . SER   B 80  ? 0.1415 0.1378 0.1654 0.0103  0.0001  0.0067  80  SER   B C   
5121 O  O   . SER   B 80  ? 0.1543 0.1362 0.1971 0.0128  0.0075  0.0032  80  SER   B O   
5122 C  CB  . SER   B 80  ? 0.1436 0.1440 0.1757 -0.0031 0.0029  0.0115  80  SER   B CB  
5123 O  OG  . SER   B 80  ? 0.1518 0.1579 0.1926 0.0005  -0.0059 0.0104  80  SER   B OG  
5129 N  N   . CYS   B 81  ? 0.1425 0.1280 0.1660 0.0018  -0.0038 0.0002  81  CYS   B N   
5130 C  CA  . CYS   B 81  ? 0.1484 0.1271 0.1602 0.0051  -0.0089 -0.0018 81  CYS   B CA  
5131 C  C   . CYS   B 81  ? 0.1452 0.1216 0.1410 0.0016  -0.0163 -0.0040 81  CYS   B C   
5132 O  O   . CYS   B 81  ? 0.1660 0.1262 0.1608 0.0061  -0.0017 0.0007  81  CYS   B O   
5133 C  CB  . CYS   B 81  ? 0.1628 0.1383 0.1666 -0.0009 -0.0157 0.0001  81  CYS   B CB  
5134 S  SG  . CYS   B 81  ? 0.1623 0.1571 0.1678 -0.0042 -0.0236 -0.0081 81  CYS   B SG  
5140 N  N   . VAL   B 82  ? 0.1495 0.1215 0.1557 -0.0048 -0.0191 -0.0054 82  VAL   B N   
5141 C  CA  . VAL   B 82  ? 0.1535 0.1337 0.1517 -0.0080 -0.0106 0.0061  82  VAL   B CA  
5142 C  C   . VAL   B 82  ? 0.1569 0.1238 0.1621 -0.0066 -0.0043 0.0014  82  VAL   B C   
5143 O  O   . VAL   B 82  ? 0.1678 0.1255 0.1904 -0.0068 -0.0068 -0.0118 82  VAL   B O   
5144 C  CB  . VAL   B 82  ? 0.1596 0.1521 0.1684 -0.0035 -0.0157 0.0065  82  VAL   B CB  
5145 C  CG1 . VAL   B 82  ? 0.1852 0.1726 0.1779 -0.0015 -0.0169 0.0157  82  VAL   B CG1 
5146 C  CG2 . VAL   B 82  ? 0.1651 0.1626 0.1825 -0.0048 -0.0274 0.0081  82  VAL   B CG2 
5156 N  N   . LEU   B 83  ? 0.1424 0.1260 0.1598 -0.0140 -0.0224 -0.0069 83  LEU   B N   
5157 C  CA  . LEU   B 83  ? 0.1496 0.1309 0.1494 -0.0149 -0.0203 0.0006  83  LEU   B CA  
5158 C  C   . LEU   B 83  ? 0.1476 0.1295 0.1492 -0.0197 -0.0197 -0.0001 83  LEU   B C   
5159 O  O   . LEU   B 83  ? 0.1507 0.1375 0.1363 -0.0211 -0.0125 0.0022  83  LEU   B O   
5160 C  CB  . LEU   B 83  ? 0.1530 0.1433 0.1486 -0.0135 -0.0260 -0.0049 83  LEU   B CB  
5161 C  CG  . LEU   B 83  ? 0.1742 0.1628 0.1596 -0.0210 -0.0174 -0.0019 83  LEU   B CG  
5162 C  CD1 . LEU   B 83  ? 0.1853 0.1675 0.1588 -0.0189 -0.0232 0.0061  83  LEU   B CD1 
5163 C  CD2 . LEU   B 83  ? 0.1982 0.1676 0.1752 -0.0118 -0.0150 -0.0160 83  LEU   B CD2 
5175 N  N   . SER   B 84  ? 0.1529 0.1389 0.1721 -0.0266 -0.0214 0.0074  84  SER   B N   
5176 C  CA  . SER   B 84  ? 0.1543 0.1606 0.1572 -0.0253 -0.0123 0.0157  84  SER   B CA  
5177 C  C   . SER   B 84  ? 0.1456 0.1773 0.1199 -0.0252 -0.0121 0.0228  84  SER   B C   
5178 O  O   . SER   B 84  ? 0.1528 0.1601 0.1284 -0.0198 -0.0123 0.0044  84  SER   B O   
5179 C  CB  . SER   B 84  ? 0.1723 0.1624 0.2091 -0.0259 0.0068  0.0115  84  SER   B CB  
5180 O  OG  . SER   B 84  ? 0.1717 0.1764 0.2545 -0.0384 0.0090  0.0176  84  SER   B OG  
5186 N  N   . GLY   B 85  ? 0.1485 0.1961 0.1429 -0.0302 -0.0118 0.0254  85  GLY   B N   
5187 C  CA  . GLY   B 85  ? 0.1538 0.1992 0.1696 -0.0354 -0.0032 -0.0023 85  GLY   B CA  
5188 C  C   . GLY   B 85  ? 0.1494 0.1849 0.1535 -0.0416 -0.0064 0.0052  85  GLY   B C   
5189 O  O   . GLY   B 85  ? 0.1556 0.1825 0.1636 -0.0517 0.0109  -0.0071 85  GLY   B O   
5193 N  N   . HIS   B 86  ? 0.1500 0.1697 0.1613 -0.0305 -0.0149 0.0163  86  HIS   B N   
5194 C  CA  . HIS   B 86  ? 0.1523 0.1703 0.1552 -0.0287 -0.0200 0.0159  86  HIS   B CA  
5195 C  C   . HIS   B 86  ? 0.1545 0.1821 0.1455 -0.0459 -0.0031 0.0271  86  HIS   B C   
5196 O  O   . HIS   B 86  ? 0.1743 0.1910 0.1545 -0.0369 0.0064  0.0202  86  HIS   B O   
5197 C  CB  . HIS   B 86  ? 0.1632 0.1726 0.1659 -0.0204 -0.0205 0.0035  86  HIS   B CB  
5198 C  CG  . HIS   B 86  ? 0.1657 0.1820 0.1637 -0.0148 -0.0279 0.0140  86  HIS   B CG  
5199 N  ND1 . HIS   B 86  ? 0.1770 0.2035 0.1811 -0.0213 -0.0311 0.0034  86  HIS   B ND1 
5200 C  CD2 . HIS   B 86  ? 0.1674 0.1841 0.1731 -0.0110 -0.0202 0.0078  86  HIS   B CD2 
5201 C  CE1 . HIS   B 86  ? 0.1806 0.2000 0.1706 -0.0184 -0.0131 -0.0149 86  HIS   B CE1 
5202 N  NE2 . HIS   B 86  ? 0.1723 0.1912 0.1600 0.0005  -0.0094 0.0028  86  HIS   B NE2 
5210 N  N   . ASN   B 87  ? 0.1559 0.1861 0.1681 -0.0357 0.0021  0.0214  87  ASN   B N   
5211 C  CA  . ASN   B 87  ? 0.1614 0.1983 0.1717 -0.0359 0.0194  0.0221  87  ASN   B CA  
5212 C  C   . ASN   B 87  ? 0.1741 0.1845 0.1714 -0.0283 0.0321  0.0154  87  ASN   B C   
5213 O  O   . ASN   B 87  ? 0.1985 0.1915 0.2079 -0.0242 0.0453  0.0072  87  ASN   B O   
5214 C  CB  . ASN   B 87  ? 0.1631 0.2349 0.2034 -0.0296 0.0266  0.0121  87  ASN   B CB  
5215 C  CG  . ASN   B 87  ? 0.1685 0.2560 0.2113 0.0024  0.0297  0.0296  87  ASN   B CG  
5216 O  OD1 . ASN   B 87  ? 0.1623 0.2443 0.2029 0.0062  0.0401  0.0388  87  ASN   B OD1 
5217 N  ND2 . ASN   B 87  ? 0.2045 0.2702 0.2482 0.0061  0.0343  0.0297  87  ASN   B ND2 
5224 N  N   . LEU   B 88  ? 0.1605 0.1738 0.1536 -0.0333 0.0139  0.0063  88  LEU   B N   
5225 C  CA  . LEU   B 88  ? 0.1716 0.1716 0.1526 -0.0325 0.0086  0.0039  88  LEU   B CA  
5226 C  C   . LEU   B 88  ? 0.1731 0.1573 0.1582 -0.0399 -0.0051 0.0061  88  LEU   B C   
5227 O  O   . LEU   B 88  ? 0.2003 0.1664 0.1903 -0.0275 -0.0257 -0.0062 88  LEU   B O   
5228 C  CB  . LEU   B 88  ? 0.1862 0.1755 0.1724 -0.0371 -0.0096 0.0082  88  LEU   B CB  
5229 C  CG  . LEU   B 88  ? 0.2270 0.2038 0.1894 -0.0333 -0.0213 0.0263  88  LEU   B CG  
5230 C  CD1 . LEU   B 88  ? 0.2433 0.2339 0.2171 -0.0435 -0.0196 0.0361  88  LEU   B CD1 
5231 C  CD2 . LEU   B 88  ? 0.2628 0.2286 0.2495 0.0042  -0.0441 0.0070  88  LEU   B CD2 
5243 N  N   . ALA   B 89  ? 0.1604 0.1562 0.1436 -0.0387 0.0115  0.0000  89  ALA   B N   
5244 C  CA  . ALA   B 89  ? 0.1577 0.1541 0.1311 -0.0418 0.0046  0.0099  89  ALA   B CA  
5245 C  C   . ALA   B 89  ? 0.1677 0.1558 0.1377 -0.0457 0.0135  0.0095  89  ALA   B C   
5246 O  O   . ALA   B 89  ? 0.1487 0.1681 0.1757 -0.0454 0.0132  -0.0231 89  ALA   B O   
5247 C  CB  . ALA   B 89  ? 0.1554 0.1598 0.1408 -0.0393 0.0000  0.0099  89  ALA   B CB  
5253 N  N   . LYS   B 90  ? 0.2047 0.1436 0.1495 -0.0489 -0.0058 0.0135  90  LYS   B N   
5254 C  CA  . LYS   B 90  ? 0.2178 0.1398 0.1440 -0.0466 -0.0118 0.0114  90  LYS   B CA  
5255 C  C   . LYS   B 90  ? 0.1983 0.1310 0.1605 -0.0444 -0.0133 0.0016  90  LYS   B C   
5256 O  O   . LYS   B 90  ? 0.2066 0.1467 0.1750 -0.0525 -0.0030 0.0028  90  LYS   B O   
5257 C  CB  . LYS   B 90  ? 0.2376 0.1444 0.1695 -0.0406 -0.0043 0.0223  90  LYS   B CB  
5258 C  CG  . LYS   B 90  ? 0.2431 0.1633 0.1735 -0.0219 0.0178  0.0179  90  LYS   B CG  
5259 C  CD  . LYS   B 90  ? 0.2727 0.1866 0.2202 -0.0152 0.0418  -0.0014 90  LYS   B CD  
5260 C  CE  . LYS   B 90  ? 0.2842 0.2036 0.2698 -0.0187 0.0591  -0.0088 90  LYS   B CE  
5261 N  NZ  . LYS   B 90  ? 0.2963 0.1941 0.2571 -0.0287 0.0798  -0.0120 90  LYS   B NZ  
5275 N  N   . HIS   B 91  ? 0.1752 0.1292 0.1459 -0.0338 -0.0197 0.0081  91  HIS   B N   
5276 C  CA  . HIS   B 91  ? 0.1614 0.1316 0.1506 -0.0259 -0.0198 0.0000  91  HIS   B CA  
5277 C  C   . HIS   B 91  ? 0.1486 0.1300 0.1326 -0.0261 0.0002  -0.0000 91  HIS   B C   
5278 O  O   . HIS   B 91  ? 0.1635 0.1352 0.1385 -0.0243 -0.0205 0.0059  91  HIS   B O   
5279 C  CB  . HIS   B 91  ? 0.1813 0.1327 0.1859 -0.0122 -0.0124 0.0139  91  HIS   B CB  
5280 C  CG  . HIS   B 91  ? 0.2264 0.1471 0.2519 0.0058  0.0169  0.0268  91  HIS   B CG  
5281 N  ND1 . HIS   B 91  ? 0.2530 0.1535 0.3109 -0.0001 0.0240  0.0111  91  HIS   B ND1 
5282 C  CD2 . HIS   B 91  ? 0.2380 0.1775 0.2973 0.0208  0.0071  0.0577  91  HIS   B CD2 
5283 C  CE1 . HIS   B 91  ? 0.2558 0.1700 0.3248 0.0152  0.0266  0.0219  91  HIS   B CE1 
5284 N  NE2 . HIS   B 91  ? 0.2495 0.1851 0.3262 0.0297  0.0198  0.0566  91  HIS   B NE2 
5292 N  N   . CYS   B 92  ? 0.1437 0.1291 0.1387 -0.0256 -0.0110 -0.0053 92  CYS   B N   
5293 C  CA  . CYS   B 92  ? 0.1425 0.1254 0.1315 -0.0215 -0.0062 -0.0001 92  CYS   B CA  
5294 C  C   . CYS   B 92  ? 0.1360 0.1209 0.1257 -0.0168 -0.0102 0.0018  92  CYS   B C   
5295 O  O   . CYS   B 92  ? 0.1414 0.1313 0.1617 -0.0179 -0.0039 -0.0004 92  CYS   B O   
5296 C  CB  . CYS   B 92  ? 0.1437 0.1392 0.1363 -0.0164 -0.0076 0.0050  92  CYS   B CB  
5297 S  SG  . CYS   B 92  ? 0.1426 0.1371 0.1384 -0.0118 -0.0113 0.0052  92  CYS   B SG  
5303 N  N   . LEU   B 93  ? 0.1323 0.1252 0.1293 -0.0113 -0.0085 -0.0011 93  LEU   B N   
5304 C  CA  . LEU   B 93  ? 0.1290 0.1279 0.1318 -0.0035 -0.0035 0.0062  93  LEU   B CA  
5305 C  C   . LEU   B 93  ? 0.1275 0.1268 0.1189 -0.0007 -0.0017 0.0086  93  LEU   B C   
5306 O  O   . LEU   B 93  ? 0.1342 0.1174 0.1551 -0.0056 -0.0121 0.0040  93  LEU   B O   
5307 C  CB  . LEU   B 93  ? 0.1337 0.1270 0.1479 0.0026  -0.0051 0.0080  93  LEU   B CB  
5308 C  CG  . LEU   B 93  ? 0.1283 0.1388 0.1696 -0.0032 -0.0083 0.0133  93  LEU   B CG  
5309 C  CD1 . LEU   B 93  ? 0.1336 0.1450 0.1772 0.0031  -0.0064 0.0037  93  LEU   B CD1 
5310 C  CD2 . LEU   B 93  ? 0.1358 0.1406 0.1791 0.0001  -0.0106 0.0064  93  LEU   B CD2 
5322 N  N   . HIS   B 94  ? 0.1336 0.1254 0.1239 -0.0059 -0.0126 0.0087  94  HIS   B N   
5323 C  CA  . HIS   B 94  ? 0.1348 0.1231 0.1278 -0.0018 -0.0029 0.0105  94  HIS   B CA  
5324 C  C   . HIS   B 94  ? 0.1307 0.1247 0.1547 -0.0016 -0.0083 0.0052  94  HIS   B C   
5325 O  O   . HIS   B 94  ? 0.1351 0.1350 0.1861 -0.0065 0.0128  -0.0006 94  HIS   B O   
5326 C  CB  . HIS   B 94  ? 0.1347 0.1275 0.1438 -0.0021 -0.0107 -0.0004 94  HIS   B CB  
5327 C  CG  . HIS   B 94  ? 0.1381 0.1217 0.1450 -0.0052 -0.0200 0.0029  94  HIS   B CG  
5328 N  ND1 . HIS   B 94  ? 0.1409 0.1327 0.1452 -0.0047 -0.0179 0.0047  94  HIS   B ND1 
5329 C  CD2 . HIS   B 94  ? 0.1428 0.1254 0.1513 -0.0015 -0.0167 0.0039  94  HIS   B CD2 
5330 C  CE1 . HIS   B 94  ? 0.1427 0.1292 0.1446 -0.0084 -0.0154 0.0024  94  HIS   B CE1 
5331 N  NE2 . HIS   B 94  ? 0.1385 0.1328 0.1527 -0.0115 -0.0182 0.0052  94  HIS   B NE2 
5339 N  N   . VAL   B 95  ? 0.1262 0.1183 0.1547 -0.0026 -0.0040 0.0033  95  VAL   B N   
5340 C  CA  . VAL   B 95  ? 0.1269 0.1295 0.1483 -0.0003 0.0003  0.0096  95  VAL   B CA  
5341 C  C   . VAL   B 95  ? 0.1357 0.1268 0.1447 -0.0037 0.0048  0.0096  95  VAL   B C   
5342 O  O   . VAL   B 95  ? 0.1411 0.1241 0.1669 0.0066  0.0055  0.0162  95  VAL   B O   
5343 C  CB  . VAL   B 95  ? 0.1341 0.1328 0.1510 -0.0020 -0.0050 0.0078  95  VAL   B CB  
5344 C  CG1 . VAL   B 95  ? 0.1402 0.1513 0.1759 -0.0064 -0.0044 0.0148  95  VAL   B CG1 
5345 C  CG2 . VAL   B 95  ? 0.1382 0.1276 0.1489 0.0029  -0.0099 0.0127  95  VAL   B CG2 
5355 N  N   . VAL   B 96  ? 0.1490 0.1360 0.1452 0.0090  0.0107  0.0174  96  VAL   B N   
5356 C  CA  . VAL   B 96  ? 0.1553 0.1451 0.1479 0.0066  0.0030  0.0230  96  VAL   B CA  
5357 C  C   . VAL   B 96  ? 0.1571 0.1488 0.1669 0.0062  0.0140  0.0224  96  VAL   B C   
5358 O  O   . VAL   B 96  ? 0.1606 0.1547 0.1893 0.0017  0.0191  0.0098  96  VAL   B O   
5359 C  CB  . VAL   B 96  ? 0.1636 0.1669 0.1450 0.0063  0.0074  0.0152  96  VAL   B CB  
5360 C  CG1 . VAL   B 96  ? 0.1651 0.1787 0.1574 0.0134  0.0114  0.0097  96  VAL   B CG1 
5361 C  CG2 . VAL   B 96  ? 0.1688 0.1683 0.1616 -0.0026 0.0114  0.0071  96  VAL   B CG2 
5371 N  N   . GLY   B 97  ? 0.1628 0.1476 0.1497 0.0029  0.0062  0.0296  97  GLY   B N   
5372 C  CA  . GLY   B 97  ? 0.1859 0.1502 0.1621 0.0009  0.0093  0.0270  97  GLY   B CA  
5373 C  C   . GLY   B 97  ? 0.2046 0.1633 0.1745 0.0142  0.0024  0.0254  97  GLY   B C   
5374 O  O   . GLY   B 97  ? 0.2224 0.1681 0.1728 0.0018  0.0034  0.0156  97  GLY   B O   
5378 N  N   . PRO   B 98  ? 0.2179 0.1702 0.1967 0.0121  0.0338  0.0361  98  PRO   B N   
5379 C  CA  . PRO   B 98  ? 0.2290 0.1890 0.2034 0.0246  0.0476  0.0311  98  PRO   B CA  
5380 C  C   . PRO   B 98  ? 0.2431 0.1924 0.1743 0.0393  0.0544  0.0500  98  PRO   B C   
5381 O  O   . PRO   B 98  ? 0.2333 0.1859 0.1951 0.0269  0.0460  0.0502  98  PRO   B O   
5382 C  CB  . PRO   B 98  ? 0.2180 0.1939 0.2151 0.0172  0.0601  0.0378  98  PRO   B CB  
5383 C  CG  . PRO   B 98  ? 0.2151 0.1836 0.2146 0.0164  0.0507  0.0494  98  PRO   B CG  
5384 C  CD  . PRO   B 98  ? 0.2046 0.1744 0.2097 0.0170  0.0437  0.0464  98  PRO   B CD  
5392 N  N   . ASN   B 99  ? 0.2573 0.2114 0.1889 0.0579  0.0534  0.0338  99  ASN   B N   
5393 C  CA  . ASN   B 99  ? 0.2800 0.2250 0.1924 0.0671  0.0497  0.0587  99  ASN   B CA  
5394 C  C   . ASN   B 99  ? 0.3140 0.2651 0.2373 0.0665  0.0634  0.0969  99  ASN   B C   
5395 O  O   . ASN   B 99  ? 0.3263 0.2736 0.2404 0.0728  0.0549  0.1033  99  ASN   B O   
5396 C  CB  . ASN   B 99  ? 0.2888 0.2175 0.1944 0.0675  0.0381  0.0450  99  ASN   B CB  
5397 C  CG  . ASN   B 99  ? 0.2938 0.2224 0.2124 0.0608  0.0323  0.0404  99  ASN   B CG  
5398 O  OD1 . ASN   B 99  ? 0.2936 0.2241 0.2491 0.0680  0.0388  0.0464  99  ASN   B OD1 
5399 N  ND2 . ASN   B 99  ? 0.2927 0.2189 0.2048 0.0599  0.0089  0.0315  99  ASN   B ND2 
5406 N  N   A VAL   B 100 ? 0.3314 0.2793 0.2829 0.0512  0.0715  0.1215  100 VAL   B N   
5407 N  N   B VAL   B 100 ? 0.3371 0.2817 0.2797 0.0553  0.0553  0.1094  100 VAL   B N   
5408 C  CA  A VAL   B 100 ? 0.3601 0.2989 0.3368 0.0385  0.0669  0.1388  100 VAL   B CA  
5409 C  CA  B VAL   B 100 ? 0.3641 0.2987 0.3205 0.0457  0.0441  0.1191  100 VAL   B CA  
5410 C  C   A VAL   B 100 ? 0.3838 0.3058 0.3314 0.0448  0.0590  0.1490  100 VAL   B C   
5411 C  C   B VAL   B 100 ? 0.3845 0.3058 0.3238 0.0490  0.0414  0.1366  100 VAL   B C   
5412 O  O   A VAL   B 100 ? 0.3917 0.3146 0.3365 0.0427  0.0677  0.1439  100 VAL   B O   
5413 O  O   B VAL   B 100 ? 0.3888 0.3102 0.3238 0.0472  0.0430  0.1331  100 VAL   B O   
5414 C  CB  A VAL   B 100 ? 0.3689 0.3123 0.3991 0.0166  0.0667  0.1507  100 VAL   B CB  
5415 C  CB  B VAL   B 100 ? 0.3716 0.3080 0.3579 0.0328  0.0368  0.1137  100 VAL   B CB  
5416 C  CG1 A VAL   B 100 ? 0.3750 0.3186 0.4277 0.0147  0.0644  0.1483  100 VAL   B CG1 
5417 C  CG1 B VAL   B 100 ? 0.3752 0.3113 0.3732 0.0307  0.0342  0.1101  100 VAL   B CG1 
5418 C  CG2 A VAL   B 100 ? 0.3696 0.3160 0.4173 0.0056  0.0689  0.1605  100 VAL   B CG2 
5419 C  CG2 B VAL   B 100 ? 0.3734 0.3112 0.3707 0.0274  0.0345  0.1129  100 VAL   B CG2 
5438 N  N   . ASN   B 101 ? 0.3990 0.3092 0.3276 0.0559  0.0383  0.1509  101 ASN   B N   
5439 C  CA  . ASN   B 101 ? 0.4363 0.3276 0.3307 0.0650  0.0179  0.1529  101 ASN   B CA  
5440 C  C   . ASN   B 101 ? 0.4774 0.3677 0.3336 0.0629  0.0115  0.1635  101 ASN   B C   
5441 O  O   . ASN   B 101 ? 0.4817 0.3812 0.3573 0.0678  0.0169  0.1362  101 ASN   B O   
5442 C  CB  . ASN   B 101 ? 0.4353 0.3102 0.3435 0.0675  0.0170  0.1329  101 ASN   B CB  
5443 C  CG  . ASN   B 101 ? 0.4340 0.2925 0.3499 0.0696  0.0209  0.1267  101 ASN   B CG  
5444 O  OD1 . ASN   B 101 ? 0.4346 0.2909 0.3676 0.0617  0.0366  0.1162  101 ASN   B OD1 
5445 N  ND2 . ASN   B 101 ? 0.4323 0.2837 0.3463 0.0742  0.0223  0.1151  101 ASN   B ND2 
5453 N  N   . LYS   B 102 ? 0.5113 0.4021 0.3600 0.0506  0.0152  0.1638  102 LYS   B N   
5454 C  CA  . LYS   B 102 ? 0.5420 0.4436 0.3972 0.0332  0.0243  0.1340  102 LYS   B CA  
5455 C  C   . LYS   B 102 ? 0.5385 0.4467 0.3764 0.0294  0.0286  0.1397  102 LYS   B C   
5456 O  O   . LYS   B 102 ? 0.5472 0.4510 0.3840 0.0293  0.0129  0.1385  102 LYS   B O   
5457 C  CB  . LYS   B 102 ? 0.5713 0.4797 0.4642 0.0211  0.0366  0.0877  102 LYS   B CB  
5458 C  CG  . LYS   B 102 ? 0.5962 0.5112 0.5223 0.0115  0.0502  0.0451  102 LYS   B CG  
5459 C  CD  . LYS   B 102 ? 0.6175 0.5368 0.5848 0.0052  0.0639  0.0106  102 LYS   B CD  
5460 C  CE  . LYS   B 102 ? 0.6331 0.5548 0.6282 0.0006  0.0715  -0.0144 102 LYS   B CE  
5461 N  NZ  . LYS   B 102 ? 0.6419 0.5653 0.6555 -0.0010 0.0724  -0.0279 102 LYS   B NZ  
5475 N  N   . GLY   B 103 ? 0.5222 0.4418 0.3755 0.0255  0.0475  0.1338  103 GLY   B N   
5476 C  CA  . GLY   B 103 ? 0.5028 0.4336 0.3818 0.0254  0.0624  0.1125  103 GLY   B CA  
5477 C  C   . GLY   B 103 ? 0.4799 0.4206 0.3760 0.0250  0.0756  0.0895  103 GLY   B C   
5478 O  O   . GLY   B 103 ? 0.4846 0.4273 0.3796 0.0270  0.0796  0.0886  103 GLY   B O   
5482 N  N   A GLU   B 104 ? 0.4648 0.4072 0.3633 0.0255  0.0917  0.0775  104 GLU   B N   
5483 N  N   B GLU   B 104 ? 0.4638 0.4112 0.3744 0.0209  0.0665  0.0715  104 GLU   B N   
5484 C  CA  A GLU   B 104 ? 0.4478 0.3938 0.3490 0.0290  0.1030  0.0610  104 GLU   B CA  
5485 C  CA  B GLU   B 104 ? 0.4465 0.4009 0.3687 0.0176  0.0567  0.0499  104 GLU   B CA  
5486 C  C   A GLU   B 104 ? 0.4478 0.3940 0.3586 0.0124  0.1451  0.0675  104 GLU   B C   
5487 C  C   B GLU   B 104 ? 0.4403 0.3993 0.3791 0.0111  0.0680  0.0438  104 GLU   B C   
5488 O  O   A GLU   B 104 ? 0.4495 0.3991 0.3708 0.0074  0.1468  0.0669  104 GLU   B O   
5489 O  O   B GLU   B 104 ? 0.4408 0.4008 0.3839 0.0094  0.0684  0.0419  104 GLU   B O   
5490 C  CB  A GLU   B 104 ? 0.4329 0.3780 0.3395 0.0500  0.0680  0.0294  104 GLU   B CB  
5491 C  CB  B GLU   B 104 ? 0.4361 0.3911 0.3560 0.0208  0.0356  0.0300  104 GLU   B CB  
5492 C  CG  A GLU   B 104 ? 0.4176 0.3644 0.3246 0.0719  0.0320  -0.0044 104 GLU   B CG  
5493 C  CG  B GLU   B 104 ? 0.4270 0.3829 0.3433 0.0247  0.0148  0.0092  104 GLU   B CG  
5494 C  CD  A GLU   B 104 ? 0.4027 0.3499 0.3050 0.0938  -0.0008 -0.0279 104 GLU   B CD  
5495 C  CD  B GLU   B 104 ? 0.4200 0.3754 0.3309 0.0282  -0.0032 -0.0057 104 GLU   B CD  
5496 O  OE1 A GLU   B 104 ? 0.3900 0.3362 0.2659 0.1089  -0.0005 -0.0332 104 GLU   B OE1 
5497 O  OE1 B GLU   B 104 ? 0.4163 0.3706 0.3160 0.0294  -0.0048 -0.0087 104 GLU   B OE1 
5498 O  OE2 A GLU   B 104 ? 0.4007 0.3500 0.2979 0.0973  -0.0254 -0.0445 104 GLU   B OE2 
5499 O  OE2 B GLU   B 104 ? 0.4180 0.3740 0.3265 0.0296  -0.0155 -0.0142 104 GLU   B OE2 
5512 N  N   A ASP   B 105 ? 0.4416 0.3876 0.3502 0.0026  0.1796  0.0717  105 ASP   B N   
5513 N  N   B ASP   B 105 ? 0.4318 0.3950 0.3774 0.0069  0.0770  0.0388  105 ASP   B N   
5514 C  CA  A ASP   B 105 ? 0.4408 0.3855 0.3699 -0.0044 0.1988  0.0554  105 ASP   B CA  
5515 C  CA  B ASP   B 105 ? 0.4257 0.3915 0.3865 0.0030  0.0816  0.0283  105 ASP   B CA  
5516 C  C   A ASP   B 105 ? 0.4213 0.3595 0.3372 -0.0177 0.2057  0.0558  105 ASP   B C   
5517 C  C   B ASP   B 105 ? 0.4153 0.3808 0.3670 -0.0022 0.0842  0.0233  105 ASP   B C   
5518 O  O   A ASP   B 105 ? 0.4084 0.3535 0.3199 -0.0195 0.2006  0.0564  105 ASP   B O   
5519 O  O   B ASP   B 105 ? 0.4150 0.3795 0.3560 -0.0024 0.0879  0.0248  105 ASP   B O   
5520 C  CB  A ASP   B 105 ? 0.4570 0.4065 0.4338 0.0042  0.2011  0.0332  105 ASP   B CB  
5521 C  CB  B ASP   B 105 ? 0.4284 0.3976 0.4141 0.0053  0.0828  0.0220  105 ASP   B CB  
5522 C  CG  A ASP   B 105 ? 0.4711 0.4253 0.4995 0.0079  0.2060  0.0181  105 ASP   B CG  
5523 C  CG  B ASP   B 105 ? 0.4314 0.4025 0.4440 0.0056  0.0853  0.0183  105 ASP   B CG  
5524 O  OD1 A ASP   B 105 ? 0.4705 0.4297 0.5064 0.0018  0.2208  0.0236  105 ASP   B OD1 
5525 O  OD1 B ASP   B 105 ? 0.4311 0.4048 0.4493 0.0029  0.0879  0.0190  105 ASP   B OD1 
5526 O  OD2 A ASP   B 105 ? 0.4789 0.4353 0.5325 0.0147  0.1990  0.0036  105 ASP   B OD2 
5527 O  OD2 B ASP   B 105 ? 0.4319 0.4042 0.4548 0.0066  0.0862  0.0164  105 ASP   B OD2 
5536 N  N   A ILE   B 106 ? 0.4124 0.3360 0.3365 -0.0273 0.1988  0.0564  106 ILE   B N   
5537 N  N   B ILE   B 106 ? 0.4038 0.3700 0.3547 -0.0054 0.0804  0.0187  106 ILE   B N   
5538 C  CA  A ILE   B 106 ? 0.3915 0.3082 0.3425 -0.0412 0.1964  0.0530  106 ILE   B CA  
5539 C  CA  B ILE   B 106 ? 0.3898 0.3588 0.3503 -0.0089 0.0787  0.0133  106 ILE   B CA  
5540 C  C   A ILE   B 106 ? 0.3566 0.2979 0.3360 -0.0331 0.1922  0.0374  106 ILE   B C   
5541 C  C   B ILE   B 106 ? 0.3696 0.3504 0.3450 -0.0055 0.0786  0.0074  106 ILE   B C   
5542 O  O   A ILE   B 106 ? 0.3425 0.2758 0.3373 -0.0375 0.1893  0.0332  106 ILE   B O   
5543 O  O   B ILE   B 106 ? 0.3666 0.3454 0.3426 -0.0075 0.0766  0.0046  106 ILE   B O   
5544 C  CB  A ILE   B 106 ? 0.4106 0.2981 0.3642 -0.0536 0.1863  0.0576  106 ILE   B CB  
5545 C  CB  B ILE   B 106 ? 0.3962 0.3578 0.3536 -0.0145 0.0766  0.0129  106 ILE   B CB  
5546 C  CG1 A ILE   B 106 ? 0.4193 0.2974 0.3723 -0.0456 0.1758  0.0460  106 ILE   B CG1 
5547 C  CG1 B ILE   B 106 ? 0.3978 0.3563 0.3546 -0.0141 0.0736  0.0116  106 ILE   B CG1 
5548 C  CG2 A ILE   B 106 ? 0.4168 0.2964 0.3776 -0.0649 0.1868  0.0662  106 ILE   B CG2 
5549 C  CG2 B ILE   B 106 ? 0.3993 0.3600 0.3589 -0.0174 0.0777  0.0131  106 ILE   B CG2 
5550 C  CD1 A ILE   B 106 ? 0.4227 0.2984 0.3698 -0.0399 0.1712  0.0428  106 ILE   B CD1 
5551 C  CD1 B ILE   B 106 ? 0.3984 0.3554 0.3555 -0.0131 0.0714  0.0111  106 ILE   B CD1 
5574 N  N   A GLN   B 107 ? 0.3377 0.3121 0.3463 -0.0263 0.1826  0.0340  107 GLN   B N   
5575 N  N   B GLN   B 107 ? 0.3534 0.3481 0.3512 -0.0022 0.0802  0.0060  107 GLN   B N   
5576 C  CA  A GLN   B 107 ? 0.3170 0.3268 0.3629 -0.0224 0.1607  0.0299  107 GLN   B CA  
5577 C  CA  B GLN   B 107 ? 0.3369 0.3443 0.3581 0.0007  0.0797  0.0082  107 GLN   B CA  
5578 C  C   A GLN   B 107 ? 0.2878 0.3061 0.3303 -0.0105 0.1276  0.0179  107 GLN   B C   
5579 C  C   B GLN   B 107 ? 0.3034 0.3175 0.3257 0.0049  0.0883  0.0088  107 GLN   B C   
5580 O  O   A GLN   B 107 ? 0.2790 0.3072 0.3532 -0.0043 0.1045  -0.0015 107 GLN   B O   
5581 O  O   B GLN   B 107 ? 0.3019 0.3203 0.3311 0.0073  0.0789  0.0008  107 GLN   B O   
5582 C  CB  A GLN   B 107 ? 0.3449 0.3661 0.4326 -0.0201 0.1341  0.0285  107 GLN   B CB  
5583 C  CB  B GLN   B 107 ? 0.3560 0.3667 0.4064 0.0012  0.0655  0.0085  107 GLN   B CB  
5584 C  CG  A GLN   B 107 ? 0.3750 0.4021 0.4998 -0.0147 0.0956  0.0260  107 GLN   B CG  
5585 C  CG  B GLN   B 107 ? 0.3730 0.3862 0.4516 0.0020  0.0485  0.0090  107 GLN   B CG  
5586 C  CD  A GLN   B 107 ? 0.3974 0.4306 0.5538 -0.0142 0.0685  0.0263  107 GLN   B CD  
5587 C  CD  B GLN   B 107 ? 0.3857 0.4011 0.4895 0.0009  0.0356  0.0098  107 GLN   B CD  
5588 O  OE1 A GLN   B 107 ? 0.4068 0.4409 0.5733 -0.0154 0.0644  0.0223  107 GLN   B OE1 
5589 O  OE1 B GLN   B 107 ? 0.3899 0.4062 0.5020 -0.0004 0.0337  0.0087  107 GLN   B OE1 
5590 N  NE2 A GLN   B 107 ? 0.4051 0.4394 0.5708 -0.0103 0.0558  0.0306  107 GLN   B NE2 
5591 N  NE2 B GLN   B 107 ? 0.3906 0.4064 0.5023 0.0023  0.0300  0.0117  107 GLN   B NE2 
5608 N  N   . LEU   B 108 ? 0.2703 0.2871 0.3012 0.0122  0.1039  0.0142  108 LEU   B N   
5609 C  CA  . LEU   B 108 ? 0.2401 0.2511 0.2573 0.0272  0.0818  0.0277  108 LEU   B CA  
5610 C  C   . LEU   B 108 ? 0.2004 0.2007 0.2478 0.0236  0.0535  0.0317  108 LEU   B C   
5611 O  O   . LEU   B 108 ? 0.1955 0.1875 0.2363 0.0166  0.0419  0.0249  108 LEU   B O   
5612 C  CB  . LEU   B 108 ? 0.2554 0.2677 0.2436 0.0285  0.0789  0.0421  108 LEU   B CB  
5613 C  CG  . LEU   B 108 ? 0.2668 0.2963 0.2531 0.0317  0.0752  0.0244  108 LEU   B CG  
5614 C  CD1 . LEU   B 108 ? 0.2782 0.3073 0.2335 0.0258  0.0793  0.0259  108 LEU   B CD1 
5615 C  CD2 . LEU   B 108 ? 0.2748 0.3090 0.2608 0.0401  0.0652  0.0087  108 LEU   B CD2 
5628 N  N   . LEU   B 109 ? 0.1830 0.1769 0.2462 0.0101  0.0438  0.0284  109 LEU   B N   
5629 C  CA  . LEU   B 109 ? 0.1619 0.1529 0.2540 0.0088  0.0414  0.0362  109 LEU   B CA  
5630 C  C   . LEU   B 109 ? 0.1504 0.1401 0.2522 0.0070  0.0408  0.0248  109 LEU   B C   
5631 O  O   . LEU   B 109 ? 0.1476 0.1374 0.2368 0.0041  0.0357  0.0311  109 LEU   B O   
5632 C  CB  . LEU   B 109 ? 0.1645 0.1425 0.2632 0.0023  0.0333  0.0411  109 LEU   B CB  
5633 C  CG  . LEU   B 109 ? 0.1602 0.1449 0.2583 0.0043  0.0255  0.0293  109 LEU   B CG  
5634 C  CD1 . LEU   B 109 ? 0.1544 0.1531 0.2417 0.0123  0.0264  0.0319  109 LEU   B CD1 
5635 C  CD2 . LEU   B 109 ? 0.1721 0.1452 0.2731 0.0082  0.0188  0.0254  109 LEU   B CD2 
5647 N  N   . LYS   B 110 ? 0.1469 0.1395 0.2530 -0.0034 0.0360  0.0180  110 LYS   B N   
5648 C  CA  . LYS   B 110 ? 0.1457 0.1347 0.2499 -0.0030 0.0276  0.0167  110 LYS   B CA  
5649 C  C   . LYS   B 110 ? 0.1417 0.1360 0.2371 0.0001  0.0325  0.0147  110 LYS   B C   
5650 O  O   . LYS   B 110 ? 0.1383 0.1383 0.2342 -0.0062 0.0232  0.0105  110 LYS   B O   
5651 C  CB  . LYS   B 110 ? 0.1396 0.1364 0.2665 -0.0045 0.0301  0.0146  110 LYS   B CB  
5652 C  CG  . LYS   B 110 ? 0.1458 0.1391 0.2823 -0.0067 0.0112  0.0163  110 LYS   B CG  
5653 C  CD  . LYS   B 110 ? 0.1455 0.1408 0.2811 -0.0131 0.0126  0.0131  110 LYS   B CD  
5654 C  CE  . LYS   B 110 ? 0.1410 0.1592 0.3044 -0.0092 0.0189  0.0068  110 LYS   B CE  
5655 N  NZ  . LYS   B 110 ? 0.1480 0.1696 0.2921 -0.0047 0.0121  0.0044  110 LYS   B NZ  
5669 N  N   . SER   B 111 ? 0.1472 0.1375 0.2513 -0.0020 0.0341  0.0167  111 SER   B N   
5670 C  CA  . SER   B 111 ? 0.1521 0.1356 0.2309 0.0014  0.0299  0.0218  111 SER   B CA  
5671 C  C   . SER   B 111 ? 0.1466 0.1314 0.2175 0.0005  0.0195  0.0132  111 SER   B C   
5672 O  O   . SER   B 111 ? 0.1391 0.1385 0.2256 -0.0005 0.0105  0.0098  111 SER   B O   
5673 C  CB  . SER   B 111 ? 0.1648 0.1563 0.2441 0.0061  0.0400  0.0206  111 SER   B CB  
5674 O  OG  . SER   B 111 ? 0.1826 0.1884 0.2543 0.0174  0.0487  0.0264  111 SER   B OG  
5680 N  N   . ALA   B 112 ? 0.1375 0.1392 0.2220 0.0077  0.0270  0.0205  112 ALA   B N   
5681 C  CA  . ALA   B 112 ? 0.1398 0.1451 0.2066 0.0044  0.0071  0.0083  112 ALA   B CA  
5682 C  C   . ALA   B 112 ? 0.1302 0.1333 0.2007 -0.0005 0.0107  0.0046  112 ALA   B C   
5683 O  O   . ALA   B 112 ? 0.1303 0.1366 0.2092 -0.0032 0.0138  0.0045  112 ALA   B O   
5684 C  CB  . ALA   B 112 ? 0.1395 0.1490 0.2139 0.0074  0.0139  0.0199  112 ALA   B CB  
5690 N  N   . TYR   B 113 ? 0.1268 0.1234 0.2167 0.0004  0.0168  0.0085  113 TYR   B N   
5691 C  CA  . TYR   B 113 ? 0.1272 0.1190 0.2138 -0.0015 0.0106  0.0010  113 TYR   B CA  
5692 C  C   . TYR   B 113 ? 0.1246 0.1214 0.2100 -0.0080 0.0094  0.0067  113 TYR   B C   
5693 O  O   . TYR   B 113 ? 0.1294 0.1242 0.1979 -0.0074 0.0035  0.0007  113 TYR   B O   
5694 C  CB  . TYR   B 113 ? 0.1320 0.1148 0.2178 -0.0008 0.0188  0.0117  113 TYR   B CB  
5695 C  CG  . TYR   B 113 ? 0.1320 0.1172 0.2349 -0.0030 0.0161  0.0165  113 TYR   B CG  
5696 C  CD1 . TYR   B 113 ? 0.1378 0.1241 0.2500 -0.0079 0.0227  0.0168  113 TYR   B CD1 
5697 C  CD2 . TYR   B 113 ? 0.1431 0.1226 0.2323 -0.0072 0.0113  0.0115  113 TYR   B CD2 
5698 C  CE1 . TYR   B 113 ? 0.1403 0.1283 0.2397 -0.0000 0.0260  0.0107  113 TYR   B CE1 
5699 C  CE2 . TYR   B 113 ? 0.1452 0.1175 0.2441 -0.0031 0.0126  0.0135  113 TYR   B CE2 
5700 C  CZ  . TYR   B 113 ? 0.1378 0.1244 0.2477 0.0009  0.0128  0.0104  113 TYR   B CZ  
5701 O  OH  . TYR   B 113 ? 0.1479 0.1187 0.2726 0.0110  0.0200  0.0107  113 TYR   B OH  
5711 N  N   . GLU   B 114 ? 0.1231 0.1160 0.2216 -0.0052 0.0131  0.0092  114 GLU   B N   
5712 C  CA  . GLU   B 114 ? 0.1227 0.1160 0.2158 0.0010  0.0059  0.0054  114 GLU   B CA  
5713 C  C   . GLU   B 114 ? 0.1234 0.1125 0.2071 -0.0019 0.0090  0.0013  114 GLU   B C   
5714 O  O   . GLU   B 114 ? 0.1244 0.1175 0.2103 0.0002  0.0036  0.0079  114 GLU   B O   
5715 C  CB  . GLU   B 114 ? 0.1272 0.1261 0.2236 -0.0019 0.0163  0.0119  114 GLU   B CB  
5716 C  CG  . GLU   B 114 ? 0.1273 0.1209 0.2333 -0.0067 0.0104  0.0050  114 GLU   B CG  
5717 C  CD  . GLU   B 114 ? 0.1252 0.1285 0.2431 -0.0056 0.0070  0.0073  114 GLU   B CD  
5718 O  OE1 . GLU   B 114 ? 0.1248 0.1425 0.2356 -0.0127 0.0200  0.0114  114 GLU   B OE1 
5719 O  OE2 . GLU   B 114 ? 0.1275 0.1458 0.2608 -0.0160 0.0127  0.0096  114 GLU   B OE2 
5726 N  N   . ASN   B 115 ? 0.1296 0.1075 0.2010 -0.0051 0.0004  0.0067  115 ASN   B N   
5727 C  CA  . ASN   B 115 ? 0.1312 0.1216 0.1736 -0.0078 -0.0012 0.0131  115 ASN   B CA  
5728 C  C   . ASN   B 115 ? 0.1247 0.1179 0.1796 -0.0095 -0.0091 0.0037  115 ASN   B C   
5729 O  O   . ASN   B 115 ? 0.1372 0.1166 0.1961 -0.0126 0.0023  0.0045  115 ASN   B O   
5730 C  CB  . ASN   B 115 ? 0.1405 0.1314 0.1862 -0.0093 -0.0003 0.0062  115 ASN   B CB  
5731 C  CG  . ASN   B 115 ? 0.1472 0.1381 0.1935 -0.0026 0.0009  -0.0005 115 ASN   B CG  
5732 O  OD1 . ASN   B 115 ? 0.1862 0.1491 0.2231 -0.0023 0.0129  -0.0083 115 ASN   B OD1 
5733 N  ND2 . ASN   B 115 ? 0.1445 0.1479 0.1815 -0.0048 0.0040  0.0028  115 ASN   B ND2 
5740 N  N   . PHE   B 116 ? 0.1278 0.1198 0.1729 -0.0045 -0.0040 0.0069  116 PHE   B N   
5741 C  CA  . PHE   B 116 ? 0.1308 0.1239 0.1840 -0.0092 -0.0046 0.0053  116 PHE   B CA  
5742 C  C   . PHE   B 116 ? 0.1316 0.1120 0.1870 -0.0141 -0.0114 0.0088  116 PHE   B C   
5743 O  O   . PHE   B 116 ? 0.1357 0.1245 0.1915 -0.0058 -0.0071 0.0102  116 PHE   B O   
5744 C  CB  . PHE   B 116 ? 0.1261 0.1186 0.1735 -0.0097 -0.0149 0.0102  116 PHE   B CB  
5745 C  CG  . PHE   B 116 ? 0.1221 0.1181 0.1709 -0.0094 0.0007  0.0072  116 PHE   B CG  
5746 C  CD1 . PHE   B 116 ? 0.1336 0.1240 0.1942 -0.0034 0.0003  0.0048  116 PHE   B CD1 
5747 C  CD2 . PHE   B 116 ? 0.1249 0.1298 0.1754 -0.0065 0.0001  0.0013  116 PHE   B CD2 
5748 C  CE1 . PHE   B 116 ? 0.1365 0.1286 0.1891 -0.0038 -0.0080 0.0069  116 PHE   B CE1 
5749 C  CE2 . PHE   B 116 ? 0.1252 0.1288 0.1865 -0.0053 0.0026  0.0059  116 PHE   B CE2 
5750 C  CZ  . PHE   B 116 ? 0.1227 0.1296 0.1930 -0.0100 -0.0113 0.0075  116 PHE   B CZ  
5760 N  N   . ASN   B 117 ? 0.1236 0.1191 0.2020 -0.0069 -0.0047 0.0093  117 ASN   B N   
5761 C  CA  . ASN   B 117 ? 0.1350 0.1203 0.1973 0.0002  -0.0073 0.0020  117 ASN   B CA  
5762 C  C   . ASN   B 117 ? 0.1394 0.1209 0.2017 0.0008  -0.0100 0.0029  117 ASN   B C   
5763 O  O   . ASN   B 117 ? 0.1447 0.1254 0.2418 -0.0087 -0.0289 0.0140  117 ASN   B O   
5764 C  CB  . ASN   B 117 ? 0.1348 0.1214 0.2010 -0.0004 -0.0070 0.0022  117 ASN   B CB  
5765 C  CG  . ASN   B 117 ? 0.1311 0.1268 0.2169 0.0030  0.0000  -0.0038 117 ASN   B CG  
5766 O  OD1 . ASN   B 117 ? 0.1474 0.1232 0.2402 -0.0111 0.0025  -0.0024 117 ASN   B OD1 
5767 N  ND2 . ASN   B 117 ? 0.1355 0.1331 0.2040 0.0011  0.0055  -0.0019 117 ASN   B ND2 
5774 N  N   . GLN   B 118 ? 0.1386 0.1166 0.1972 -0.0116 -0.0168 0.0015  118 GLN   B N   
5775 C  CA  . GLN   B 118 ? 0.1437 0.1203 0.2178 0.0002  -0.0134 0.0018  118 GLN   B CA  
5776 C  C   . GLN   B 118 ? 0.1453 0.1172 0.2196 0.0037  -0.0091 -0.0009 118 GLN   B C   
5777 O  O   . GLN   B 118 ? 0.1669 0.1135 0.2495 -0.0051 0.0020  0.0054  118 GLN   B O   
5778 C  CB  . GLN   B 118 ? 0.1468 0.1239 0.2262 0.0002  -0.0163 0.0047  118 GLN   B CB  
5779 C  CG  . GLN   B 118 ? 0.1533 0.1233 0.2224 -0.0013 -0.0073 -0.0094 118 GLN   B CG  
5780 C  CD  . GLN   B 118 ? 0.1572 0.1216 0.2219 0.0000  -0.0116 -0.0148 118 GLN   B CD  
5781 O  OE1 . GLN   B 118 ? 0.1639 0.1232 0.2465 0.0015  0.0025  0.0045  118 GLN   B OE1 
5782 N  NE2 . GLN   B 118 ? 0.1672 0.1275 0.2259 0.0023  -0.0110 -0.0019 118 GLN   B NE2 
5791 N  N   . HIS   B 119 ? 0.1490 0.1232 0.1885 -0.0090 -0.0096 0.0083  119 HIS   B N   
5792 C  CA  . HIS   B 119 ? 0.1567 0.1397 0.1786 -0.0047 -0.0179 0.0108  119 HIS   B CA  
5793 C  C   . HIS   B 119 ? 0.1595 0.1367 0.1655 -0.0082 -0.0300 0.0104  119 HIS   B C   
5794 O  O   . HIS   B 119 ? 0.1648 0.1328 0.1917 -0.0251 -0.0285 0.0119  119 HIS   B O   
5795 C  CB  . HIS   B 119 ? 0.1585 0.1488 0.1871 -0.0091 -0.0180 0.0026  119 HIS   B CB  
5796 C  CG  . HIS   B 119 ? 0.1639 0.1722 0.1978 0.0048  -0.0375 -0.0119 119 HIS   B CG  
5797 N  ND1 . HIS   B 119 ? 0.1717 0.1852 0.2275 -0.0014 -0.0405 -0.0274 119 HIS   B ND1 
5798 C  CD2 . HIS   B 119 ? 0.1769 0.1909 0.2064 0.0355  -0.0472 -0.0174 119 HIS   B CD2 
5799 C  CE1 . HIS   B 119 ? 0.1934 0.2058 0.2354 0.0118  -0.0513 -0.0401 119 HIS   B CE1 
5800 N  NE2 . HIS   B 119 ? 0.1938 0.2109 0.2267 0.0288  -0.0457 -0.0399 119 HIS   B NE2 
5808 N  N   . GLU   B 120 ? 0.1782 0.1378 0.1711 -0.0136 -0.0367 0.0182  120 GLU   B N   
5809 C  CA  . GLU   B 120 ? 0.2074 0.1528 0.1895 -0.0107 -0.0518 0.0317  120 GLU   B CA  
5810 C  C   . GLU   B 120 ? 0.1837 0.1412 0.1854 -0.0179 -0.0414 0.0261  120 GLU   B C   
5811 O  O   . GLU   B 120 ? 0.1797 0.1539 0.1893 -0.0189 -0.0391 0.0133  120 GLU   B O   
5812 C  CB  . GLU   B 120 ? 0.2710 0.1863 0.2580 0.0109  -0.0850 0.0611  120 GLU   B CB  
5813 C  CG  . GLU   B 120 ? 0.3284 0.2711 0.3545 0.0216  -0.1030 0.0835  120 GLU   B CG  
5814 C  CD  . GLU   B 120 ? 0.3747 0.3406 0.4579 0.0291  -0.1080 0.0893  120 GLU   B CD  
5815 O  OE1 . GLU   B 120 ? 0.3960 0.3782 0.4944 0.0231  -0.1043 0.0978  120 GLU   B OE1 
5816 O  OE2 . GLU   B 120 ? 0.3934 0.3831 0.5087 0.0319  -0.1041 0.0794  120 GLU   B OE2 
5823 N  N   . VAL   B 121 ? 0.1734 0.1376 0.1850 -0.0256 -0.0232 0.0200  121 VAL   B N   
5824 C  CA  . VAL   B 121 ? 0.1675 0.1452 0.1640 -0.0215 -0.0236 0.0204  121 VAL   B CA  
5825 C  C   . VAL   B 121 ? 0.1626 0.1402 0.1585 -0.0255 -0.0207 0.0180  121 VAL   B C   
5826 O  O   . VAL   B 121 ? 0.1704 0.1346 0.1825 -0.0337 -0.0248 0.0095  121 VAL   B O   
5827 C  CB  . VAL   B 121 ? 0.1872 0.1867 0.1693 -0.0100 -0.0265 0.0225  121 VAL   B CB  
5828 C  CG1 . VAL   B 121 ? 0.1952 0.2005 0.2038 -0.0176 -0.0223 0.0201  121 VAL   B CG1 
5829 C  CG2 . VAL   B 121 ? 0.2119 0.2156 0.1694 0.0006  -0.0172 0.0107  121 VAL   B CG2 
5839 N  N   . LEU   B 122 ? 0.1524 0.1354 0.1536 -0.0197 -0.0260 0.0125  122 LEU   B N   
5840 C  CA  . LEU   B 122 ? 0.1448 0.1410 0.1421 -0.0219 -0.0233 0.0120  122 LEU   B CA  
5841 C  C   . LEU   B 122 ? 0.1467 0.1334 0.1499 -0.0269 -0.0207 0.0064  122 LEU   B C   
5842 O  O   . LEU   B 122 ? 0.1524 0.1350 0.1826 -0.0290 -0.0251 0.0006  122 LEU   B O   
5843 C  CB  . LEU   B 122 ? 0.1701 0.1495 0.1808 -0.0066 -0.0334 0.0138  122 LEU   B CB  
5844 C  CG  . LEU   B 122 ? 0.1548 0.1549 0.1972 -0.0157 -0.0179 0.0117  122 LEU   B CG  
5845 C  CD1 . LEU   B 122 ? 0.1624 0.1805 0.1943 -0.0258 -0.0199 0.0053  122 LEU   B CD1 
5846 C  CD2 . LEU   B 122 ? 0.1534 0.1578 0.1693 -0.0121 -0.0131 -0.0084 122 LEU   B CD2 
5858 N  N   . LEU   B 123 ? 0.1476 0.1206 0.1473 -0.0264 -0.0183 0.0105  123 LEU   B N   
5859 C  CA  . LEU   B 123 ? 0.1481 0.1240 0.1518 -0.0260 -0.0211 0.0003  123 LEU   B CA  
5860 C  C   . LEU   B 123 ? 0.1450 0.1222 0.1482 -0.0251 -0.0226 0.0002  123 LEU   B C   
5861 O  O   . LEU   B 123 ? 0.1515 0.1259 0.1439 -0.0311 -0.0194 0.0019  123 LEU   B O   
5862 C  CB  . LEU   B 123 ? 0.1536 0.1276 0.1656 -0.0240 -0.0152 -0.0047 123 LEU   B CB  
5863 C  CG  . LEU   B 123 ? 0.1509 0.1336 0.1743 -0.0149 -0.0067 0.0068  123 LEU   B CG  
5864 C  CD1 . LEU   B 123 ? 0.1644 0.1355 0.1813 -0.0158 0.0006  -0.0056 123 LEU   B CD1 
5865 C  CD2 . LEU   B 123 ? 0.1554 0.1472 0.1921 -0.0170 -0.0012 0.0179  123 LEU   B CD2 
5877 N  N   . ALA   B 124 ? 0.1409 0.1191 0.1564 -0.0215 -0.0083 -0.0021 124 ALA   B N   
5878 C  CA  . ALA   B 124 ? 0.1340 0.1259 0.1661 -0.0159 -0.0119 -0.0117 124 ALA   B CA  
5879 C  C   . ALA   B 124 ? 0.1291 0.1253 0.1618 -0.0168 -0.0067 -0.0036 124 ALA   B C   
5880 O  O   . ALA   B 124 ? 0.1396 0.1237 0.1689 -0.0125 -0.0143 0.0030  124 ALA   B O   
5881 C  CB  . ALA   B 124 ? 0.1377 0.1337 0.1662 -0.0094 0.0002  -0.0078 124 ALA   B CB  
5887 N  N   . PRO   B 125 ? 0.1401 0.1240 0.1571 -0.0139 -0.0116 0.0110  125 PRO   B N   
5888 C  CA  . PRO   B 125 ? 0.1492 0.1222 0.1698 -0.0146 -0.0119 0.0214  125 PRO   B CA  
5889 C  C   . PRO   B 125 ? 0.1425 0.1189 0.1797 -0.0120 -0.0095 0.0088  125 PRO   B C   
5890 O  O   . PRO   B 125 ? 0.1465 0.1241 0.1905 -0.0103 -0.0016 0.0155  125 PRO   B O   
5891 C  CB  . PRO   B 125 ? 0.1522 0.1509 0.1818 -0.0197 -0.0159 0.0349  125 PRO   B CB  
5892 C  CG  . PRO   B 125 ? 0.1557 0.1530 0.1728 -0.0285 -0.0199 0.0178  125 PRO   B CG  
5893 C  CD  . PRO   B 125 ? 0.1472 0.1374 0.1608 -0.0289 -0.0095 0.0101  125 PRO   B CD  
5901 N  N   . LEU   B 126 ? 0.1476 0.1174 0.2061 -0.0170 0.0072  0.0144  126 LEU   B N   
5902 C  CA  . LEU   B 126 ? 0.1524 0.1291 0.2114 -0.0095 0.0206  0.0164  126 LEU   B CA  
5903 C  C   . LEU   B 126 ? 0.1447 0.1403 0.2184 0.0006  0.0269  0.0211  126 LEU   B C   
5904 O  O   . LEU   B 126 ? 0.1670 0.1674 0.2313 0.0211  0.0021  -0.0049 126 LEU   B O   
5905 C  CB  . LEU   B 126 ? 0.1671 0.1342 0.2425 -0.0179 0.0258  0.0110  126 LEU   B CB  
5906 C  CG  . LEU   B 126 ? 0.1819 0.1434 0.2564 -0.0312 0.0195  -0.0050 126 LEU   B CG  
5907 C  CD1 . LEU   B 126 ? 0.2002 0.1511 0.3051 -0.0284 0.0153  -0.0140 126 LEU   B CD1 
5908 C  CD2 . LEU   B 126 ? 0.1870 0.1586 0.2480 -0.0347 0.0122  -0.0156 126 LEU   B CD2 
5920 N  N   . LEU   B 127 ? 0.1401 0.1293 0.2241 0.0048  0.0280  0.0168  127 LEU   B N   
5921 C  CA  . LEU   B 127 ? 0.1440 0.1395 0.2298 -0.0056 0.0332  0.0244  127 LEU   B CA  
5922 C  C   . LEU   B 127 ? 0.1436 0.1299 0.2349 0.0007  0.0215  0.0265  127 LEU   B C   
5923 O  O   . LEU   B 127 ? 0.1437 0.1348 0.2456 -0.0132 0.0146  0.0276  127 LEU   B O   
5924 C  CB  . LEU   B 127 ? 0.1574 0.1337 0.2415 -0.0001 0.0259  0.0219  127 LEU   B CB  
5925 C  CG  . LEU   B 127 ? 0.1699 0.1342 0.2552 0.0025  0.0256  0.0182  127 LEU   B CG  
5926 C  CD1 . LEU   B 127 ? 0.1780 0.1302 0.2537 0.0070  0.0217  0.0099  127 LEU   B CD1 
5927 C  CD2 . LEU   B 127 ? 0.1733 0.1412 0.2695 -0.0167 0.0227  0.0309  127 LEU   B CD2 
5939 N  N   . SER   B 128 ? 0.1464 0.1309 0.2321 0.0030  0.0084  0.0157  128 SER   B N   
5940 C  CA  . SER   B 128 ? 0.1593 0.1381 0.2330 0.0081  -0.0032 0.0288  128 SER   B CA  
5941 C  C   . SER   B 128 ? 0.1754 0.1472 0.2617 0.0095  -0.0226 0.0236  128 SER   B C   
5942 O  O   . SER   B 128 ? 0.1930 0.1524 0.2906 0.0051  -0.0228 0.0395  128 SER   B O   
5943 C  CB  . SER   B 128 ? 0.1711 0.1401 0.2359 0.0092  0.0056  0.0340  128 SER   B CB  
5944 O  OG  . SER   B 128 ? 0.1721 0.1608 0.2329 0.0134  0.0165  0.0368  128 SER   B OG  
5950 N  N   . ALA   B 129 ? 0.1903 0.1521 0.2913 0.0248  -0.0144 0.0083  129 ALA   B N   
5951 C  CA  . ALA   B 129 ? 0.2031 0.1531 0.2958 0.0317  -0.0113 0.0032  129 ALA   B CA  
5952 C  C   . ALA   B 129 ? 0.1895 0.1460 0.2772 0.0195  0.0022  0.0070  129 ALA   B C   
5953 O  O   . ALA   B 129 ? 0.1764 0.1508 0.2788 0.0173  0.0026  0.0013  129 ALA   B O   
5954 C  CB  . ALA   B 129 ? 0.2257 0.1784 0.3333 0.0374  -0.0008 0.0019  129 ALA   B CB  
5960 N  N   . GLY   B 130 ? 0.1857 0.1444 0.2790 0.0229  0.0038  0.0052  130 GLY   B N   
5961 C  CA  . GLY   B 130 ? 0.1892 0.1573 0.2860 0.0163  0.0200  0.0058  130 GLY   B CA  
5962 C  C   . GLY   B 130 ? 0.1923 0.1623 0.2800 0.0143  0.0144  0.0132  130 GLY   B C   
5963 O  O   . GLY   B 130 ? 0.2070 0.1747 0.2851 0.0157  0.0155  0.0228  130 GLY   B O   
5967 N  N   . ILE   B 131 ? 0.1867 0.1760 0.2838 0.0332  0.0147  0.0043  131 ILE   B N   
5968 C  CA  . ILE   B 131 ? 0.2112 0.1889 0.2836 0.0310  0.0024  0.0168  131 ILE   B CA  
5969 C  C   . ILE   B 131 ? 0.2245 0.1786 0.2491 0.0195  0.0046  0.0257  131 ILE   B C   
5970 O  O   . ILE   B 131 ? 0.2554 0.1960 0.2563 0.0154  -0.0105 0.0212  131 ILE   B O   
5971 C  CB  . ILE   B 131 ? 0.2122 0.2233 0.3168 0.0290  -0.0099 0.0283  131 ILE   B CB  
5972 C  CG1 . ILE   B 131 ? 0.2104 0.2474 0.3335 -0.0016 -0.0040 0.0326  131 ILE   B CG1 
5973 C  CG2 . ILE   B 131 ? 0.2180 0.2419 0.3452 0.0357  -0.0079 0.0263  131 ILE   B CG2 
5974 C  CD1 . ILE   B 131 ? 0.2116 0.2690 0.3524 -0.0195 -0.0093 0.0349  131 ILE   B CD1 
5986 N  N   . PHE   B 132 ? 0.2097 0.1608 0.2456 0.0164  0.0230  0.0286  132 PHE   B N   
5987 C  CA  . PHE   B 132 ? 0.2228 0.1651 0.2444 0.0094  0.0406  0.0211  132 PHE   B CA  
5988 C  C   . PHE   B 132 ? 0.2434 0.1798 0.2648 0.0137  0.0549  0.0161  132 PHE   B C   
5989 O  O   . PHE   B 132 ? 0.2596 0.2037 0.2852 0.0080  0.0727  0.0225  132 PHE   B O   
5990 C  CB  . PHE   B 132 ? 0.2081 0.1636 0.2196 0.0104  0.0393  0.0268  132 PHE   B CB  
5991 C  CG  . PHE   B 132 ? 0.2049 0.1664 0.2151 0.0165  0.0304  0.0258  132 PHE   B CG  
5992 C  CD1 . PHE   B 132 ? 0.2084 0.1656 0.2405 0.0202  0.0224  0.0196  132 PHE   B CD1 
5993 C  CD2 . PHE   B 132 ? 0.2060 0.1691 0.1999 0.0273  0.0266  0.0271  132 PHE   B CD2 
5994 C  CE1 . PHE   B 132 ? 0.2184 0.1724 0.2469 0.0113  0.0161  0.0204  132 PHE   B CE1 
5995 C  CE2 . PHE   B 132 ? 0.2143 0.1750 0.2058 0.0234  0.0123  0.0219  132 PHE   B CE2 
5996 C  CZ  . PHE   B 132 ? 0.2179 0.1773 0.2300 0.0120  0.0037  0.0304  132 PHE   B CZ  
6006 N  N   . GLY   B 133 ? 0.2403 0.1695 0.2607 0.0035  0.0414  0.0428  133 GLY   B N   
6007 C  CA  . GLY   B 133 ? 0.2518 0.1830 0.2686 -0.0127 0.0370  0.0467  133 GLY   B CA  
6008 C  C   . GLY   B 133 ? 0.2549 0.1920 0.2743 -0.0276 0.0426  0.0494  133 GLY   B C   
6009 O  O   . GLY   B 133 ? 0.2740 0.2013 0.3139 -0.0384 0.0491  0.0584  133 GLY   B O   
6013 N  N   . ALA   B 134 ? 0.2318 0.1904 0.2548 -0.0245 0.0425  0.0335  134 ALA   B N   
6014 C  CA  . ALA   B 134 ? 0.2214 0.1918 0.2598 -0.0158 0.0461  0.0241  134 ALA   B CA  
6015 C  C   . ALA   B 134 ? 0.2233 0.1830 0.2747 -0.0123 0.0415  0.0405  134 ALA   B C   
6016 O  O   . ALA   B 134 ? 0.2236 0.1956 0.2954 0.0031  0.0345  0.0359  134 ALA   B O   
6017 C  CB  . ALA   B 134 ? 0.2199 0.1967 0.2725 -0.0119 0.0371  0.0195  134 ALA   B CB  
6023 N  N   . ASP   B 135 ? 0.2382 0.1754 0.2834 -0.0191 0.0238  0.0407  135 ASP   B N   
6024 C  CA  . ASP   B 135 ? 0.2557 0.1663 0.2965 -0.0164 0.0086  0.0436  135 ASP   B CA  
6025 C  C   . ASP   B 135 ? 0.2332 0.1493 0.2807 -0.0040 0.0108  0.0368  135 ASP   B C   
6026 O  O   . ASP   B 135 ? 0.2205 0.1486 0.2935 -0.0036 0.0190  0.0343  135 ASP   B O   
6027 C  CB  . ASP   B 135 ? 0.2896 0.1791 0.3290 -0.0395 0.0072  0.0448  135 ASP   B CB  
6028 C  CG  . ASP   B 135 ? 0.3200 0.1792 0.3818 -0.0614 0.0065  0.0403  135 ASP   B CG  
6029 O  OD1 . ASP   B 135 ? 0.3246 0.1568 0.3880 -0.0513 0.0006  0.0362  135 ASP   B OD1 
6030 O  OD2 . ASP   B 135 ? 0.3457 0.2134 0.4258 -0.0768 0.0018  0.0173  135 ASP   B OD2 
6035 N  N   . PRO   B 136 ? 0.2227 0.1550 0.2929 0.0136  -0.0068 0.0302  136 PRO   B N   
6036 C  CA  . PRO   B 136 ? 0.2031 0.1435 0.2915 0.0131  -0.0033 0.0130  136 PRO   B CA  
6037 C  C   . PRO   B 136 ? 0.1840 0.1323 0.3082 0.0096  -0.0013 0.0141  136 PRO   B C   
6038 O  O   . PRO   B 136 ? 0.1686 0.1346 0.2928 0.0074  0.0087  0.0136  136 PRO   B O   
6039 C  CB  . PRO   B 136 ? 0.2130 0.1661 0.2959 0.0240  -0.0101 0.0074  136 PRO   B CB  
6040 C  CG  . PRO   B 136 ? 0.2307 0.1766 0.3156 0.0309  -0.0014 0.0083  136 PRO   B CG  
6041 C  CD  . PRO   B 136 ? 0.2337 0.1757 0.3029 0.0333  -0.0010 0.0129  136 PRO   B CD  
6049 N  N   . ILE   B 137 ? 0.1919 0.1249 0.3268 0.0131  -0.0089 0.0129  137 ILE   B N   
6050 C  CA  . ILE   B 137 ? 0.2005 0.1227 0.3289 -0.0024 0.0021  0.0070  137 ILE   B CA  
6051 C  C   . ILE   B 137 ? 0.1940 0.1287 0.3085 -0.0099 0.0188  0.0160  137 ILE   B C   
6052 O  O   . ILE   B 137 ? 0.1870 0.1312 0.2935 -0.0106 0.0148  0.0141  137 ILE   B O   
6053 C  CB  . ILE   B 137 ? 0.2316 0.1302 0.3788 -0.0107 0.0049  0.0067  137 ILE   B CB  
6054 C  CG1 . ILE   B 137 ? 0.2597 0.1496 0.4204 -0.0011 0.0130  -0.0028 137 ILE   B CG1 
6055 C  CG2 . ILE   B 137 ? 0.2315 0.1301 0.3927 -0.0334 0.0024  0.0097  137 ILE   B CG2 
6056 C  CD1 . ILE   B 137 ? 0.2825 0.1814 0.4591 0.0131  0.0110  0.0016  137 ILE   B CD1 
6068 N  N   . HIS   B 138 ? 0.1985 0.1318 0.3072 -0.0099 0.0279  0.0137  138 HIS   B N   
6069 C  CA  . HIS   B 138 ? 0.2077 0.1415 0.3011 -0.0081 0.0407  0.0157  138 HIS   B CA  
6070 C  C   . HIS   B 138 ? 0.1847 0.1407 0.2918 -0.0064 0.0293  0.0300  138 HIS   B C   
6071 O  O   . HIS   B 138 ? 0.1754 0.1458 0.3164 -0.0012 0.0383  0.0412  138 HIS   B O   
6072 C  CB  . HIS   B 138 ? 0.2339 0.1544 0.3159 -0.0122 0.0585  0.0100  138 HIS   B CB  
6073 C  CG  . HIS   B 138 ? 0.2588 0.1706 0.3220 -0.0158 0.0811  0.0353  138 HIS   B CG  
6074 N  ND1 . HIS   B 138 ? 0.2687 0.1881 0.3467 -0.0108 0.0971  0.0293  138 HIS   B ND1 
6075 C  CD2 . HIS   B 138 ? 0.2749 0.1770 0.3251 -0.0120 0.0857  0.0345  138 HIS   B CD2 
6076 C  CE1 . HIS   B 138 ? 0.2752 0.1871 0.3482 -0.0068 0.1003  0.0305  138 HIS   B CE1 
6077 N  NE2 . HIS   B 138 ? 0.2811 0.1787 0.3265 -0.0012 0.0957  0.0265  138 HIS   B NE2 
6085 N  N   . SER   B 139 ? 0.1808 0.1280 0.2939 0.0035  0.0237  0.0198  139 SER   B N   
6086 C  CA  . SER   B 139 ? 0.1781 0.1206 0.2785 -0.0013 0.0251  0.0144  139 SER   B CA  
6087 C  C   . SER   B 139 ? 0.1558 0.1149 0.2656 -0.0077 0.0206  0.0096  139 SER   B C   
6088 O  O   . SER   B 139 ? 0.1587 0.1225 0.2593 -0.0031 0.0119  0.0138  139 SER   B O   
6089 C  CB  . SER   B 139 ? 0.1871 0.1262 0.2796 -0.0018 0.0044  0.0118  139 SER   B CB  
6090 O  OG  . SER   B 139 ? 0.1864 0.1257 0.2777 -0.0019 -0.0029 0.0172  139 SER   B OG  
6096 N  N   . LEU   B 140 ? 0.1573 0.1147 0.2602 -0.0083 0.0210  0.0002  140 LEU   B N   
6097 C  CA  . LEU   B 140 ? 0.1544 0.1176 0.2708 -0.0017 0.0187  0.0025  140 LEU   B CA  
6098 C  C   . LEU   B 140 ? 0.1494 0.1166 0.2798 -0.0081 0.0039  0.0008  140 LEU   B C   
6099 O  O   . LEU   B 140 ? 0.1455 0.1258 0.2773 -0.0060 0.0002  0.0088  140 LEU   B O   
6100 C  CB  . LEU   B 140 ? 0.1533 0.1179 0.2766 -0.0139 0.0198  -0.0048 140 LEU   B CB  
6101 C  CG  . LEU   B 140 ? 0.1653 0.1209 0.2740 -0.0139 0.0072  0.0018  140 LEU   B CG  
6102 C  CD1 . LEU   B 140 ? 0.1698 0.1289 0.2905 -0.0141 0.0144  0.0017  140 LEU   B CD1 
6103 C  CD2 . LEU   B 140 ? 0.1791 0.1324 0.2829 -0.0173 0.0048  -0.0093 140 LEU   B CD2 
6115 N  N   . ARG   B 141 ? 0.1412 0.1200 0.2946 -0.0122 0.0093  -0.0022 141 ARG   B N   
6116 C  CA  . ARG   B 141 ? 0.1432 0.1208 0.3213 -0.0138 0.0248  -0.0063 141 ARG   B CA  
6117 C  C   . ARG   B 141 ? 0.1401 0.1232 0.3003 -0.0173 0.0145  -0.0014 141 ARG   B C   
6118 O  O   . ARG   B 141 ? 0.1482 0.1278 0.3087 -0.0129 0.0010  -0.0112 141 ARG   B O   
6119 C  CB  . ARG   B 141 ? 0.1633 0.1355 0.3423 -0.0180 0.0366  -0.0174 141 ARG   B CB  
6120 C  CG  . ARG   B 141 ? 0.1931 0.1595 0.3477 -0.0153 0.0344  -0.0156 141 ARG   B CG  
6121 C  CD  . ARG   B 141 ? 0.2346 0.1809 0.3496 -0.0152 0.0216  -0.0203 141 ARG   B CD  
6122 N  NE  . ARG   B 141 ? 0.2601 0.1798 0.3439 -0.0321 0.0264  -0.0225 141 ARG   B NE  
6123 C  CZ  . ARG   B 141 ? 0.2784 0.1667 0.3219 -0.0268 0.0319  -0.0289 141 ARG   B CZ  
6124 N  NH1 . ARG   B 141 ? 0.2896 0.1543 0.3144 -0.0257 0.0349  -0.0321 141 ARG   B NH1 
6125 N  NH2 . ARG   B 141 ? 0.2937 0.1762 0.3279 -0.0122 0.0201  -0.0140 141 ARG   B NH2 
6139 N  N   . VAL   B 142 ? 0.1440 0.1186 0.2869 -0.0116 0.0160  -0.0023 142 VAL   B N   
6140 C  CA  . VAL   B 142 ? 0.1406 0.1201 0.2836 -0.0078 0.0186  -0.0030 142 VAL   B CA  
6141 C  C   . VAL   B 142 ? 0.1397 0.1178 0.2859 -0.0014 0.0128  -0.0026 142 VAL   B C   
6142 O  O   . VAL   B 142 ? 0.1488 0.1233 0.2906 0.0013  0.0170  0.0035  142 VAL   B O   
6143 C  CB  . VAL   B 142 ? 0.1522 0.1333 0.2871 0.0009  0.0206  0.0165  142 VAL   B CB  
6144 C  CG1 . VAL   B 142 ? 0.1526 0.1317 0.2893 0.0099  0.0251  0.0048  142 VAL   B CG1 
6145 C  CG2 . VAL   B 142 ? 0.1679 0.1359 0.2911 0.0047  0.0153  0.0190  142 VAL   B CG2 
6155 N  N   . CYS   B 143 ? 0.1358 0.1227 0.2735 -0.0003 0.0078  0.0049  143 CYS   B N   
6156 C  CA  . CYS   B 143 ? 0.1310 0.1234 0.2778 -0.0089 0.0028  0.0038  143 CYS   B CA  
6157 C  C   . CYS   B 143 ? 0.1296 0.1209 0.2722 -0.0111 0.0098  0.0030  143 CYS   B C   
6158 O  O   . CYS   B 143 ? 0.1346 0.1285 0.2665 -0.0068 0.0002  -0.0053 143 CYS   B O   
6159 C  CB  . CYS   B 143 ? 0.1366 0.1320 0.2672 -0.0074 0.0046  0.0011  143 CYS   B CB  
6160 S  SG  . CYS   B 143 ? 0.1410 0.1433 0.2688 -0.0064 0.0043  0.0081  143 CYS   B SG  
6166 N  N   . VAL   B 144 ? 0.1328 0.1213 0.2814 -0.0122 0.0013  -0.0103 144 VAL   B N   
6167 C  CA  . VAL   B 144 ? 0.1411 0.1293 0.3034 -0.0148 -0.0150 -0.0168 144 VAL   B CA  
6168 C  C   . VAL   B 144 ? 0.1411 0.1327 0.3081 -0.0114 -0.0124 0.0021  144 VAL   B C   
6169 O  O   . VAL   B 144 ? 0.1461 0.1533 0.3216 -0.0048 -0.0144 0.0180  144 VAL   B O   
6170 C  CB  . VAL   B 144 ? 0.1698 0.1462 0.3550 -0.0185 -0.0237 -0.0329 144 VAL   B CB  
6171 C  CG1 . VAL   B 144 ? 0.1947 0.1874 0.3834 -0.0071 -0.0271 -0.0226 144 VAL   B CG1 
6172 C  CG2 . VAL   B 144 ? 0.1839 0.1483 0.3512 -0.0074 -0.0321 -0.0407 144 VAL   B CG2 
6182 N  N   . ASP   B 145 ? 0.1432 0.1292 0.3227 -0.0108 -0.0016 -0.0133 145 ASP   B N   
6183 C  CA  . ASP   B 145 ? 0.1431 0.1365 0.3465 -0.0092 0.0077  -0.0062 145 ASP   B CA  
6184 C  C   . ASP   B 145 ? 0.1348 0.1402 0.3293 -0.0097 0.0091  -0.0091 145 ASP   B C   
6185 O  O   . ASP   B 145 ? 0.1358 0.1552 0.3805 -0.0131 0.0112  -0.0260 145 ASP   B O   
6186 C  CB  . ASP   B 145 ? 0.1477 0.1404 0.3931 -0.0125 0.0196  -0.0078 145 ASP   B CB  
6187 C  CG  . ASP   B 145 ? 0.1644 0.1444 0.4417 -0.0247 0.0282  -0.0141 145 ASP   B CG  
6188 O  OD1 . ASP   B 145 ? 0.1724 0.1491 0.4417 -0.0281 0.0041  -0.0195 145 ASP   B OD1 
6189 O  OD2 . ASP   B 145 ? 0.1943 0.1513 0.4794 -0.0321 0.0551  -0.0022 145 ASP   B OD2 
6194 N  N   . THR   B 146 ? 0.1328 0.1267 0.2791 -0.0116 0.0092  0.0048  146 THR   B N   
6195 C  CA  . THR   B 146 ? 0.1353 0.1225 0.2650 -0.0084 0.0125  0.0028  146 THR   B CA  
6196 C  C   . THR   B 146 ? 0.1348 0.1233 0.2591 -0.0055 0.0046  0.0035  146 THR   B C   
6197 O  O   . THR   B 146 ? 0.1386 0.1239 0.2611 -0.0064 0.0045  -0.0010 146 THR   B O   
6198 C  CB  . THR   B 146 ? 0.1396 0.1207 0.2646 -0.0053 0.0244  0.0059  146 THR   B CB  
6199 O  OG1 . THR   B 146 ? 0.1470 0.1219 0.2683 -0.0072 0.0186  0.0149  146 THR   B OG1 
6200 C  CG2 . THR   B 146 ? 0.1462 0.1307 0.2680 -0.0048 0.0179  0.0013  146 THR   B CG2 
6208 N  N   . VAL   B 147 ? 0.1380 0.1262 0.2484 -0.0040 0.0163  0.0061  147 VAL   B N   
6209 C  CA  . VAL   B 147 ? 0.1401 0.1241 0.2436 -0.0103 -0.0043 0.0032  147 VAL   B CA  
6210 C  C   . VAL   B 147 ? 0.1383 0.1221 0.2474 -0.0202 -0.0102 -0.0027 147 VAL   B C   
6211 O  O   . VAL   B 147 ? 0.1486 0.1360 0.2553 -0.0181 -0.0340 -0.0019 147 VAL   B O   
6212 C  CB  . VAL   B 147 ? 0.1429 0.1350 0.2266 -0.0071 -0.0120 0.0032  147 VAL   B CB  
6213 C  CG1 . VAL   B 147 ? 0.1377 0.1483 0.2183 -0.0082 -0.0042 0.0111  147 VAL   B CG1 
6214 C  CG2 . VAL   B 147 ? 0.1416 0.1296 0.2303 -0.0089 -0.0025 -0.0021 147 VAL   B CG2 
6224 N  N   . ARG   B 148 ? 0.1420 0.1234 0.2412 -0.0101 -0.0192 -0.0066 148 ARG   B N   
6225 C  CA  . ARG   B 148 ? 0.1447 0.1353 0.2289 -0.0077 -0.0269 -0.0080 148 ARG   B CA  
6226 C  C   . ARG   B 148 ? 0.1493 0.1470 0.2127 -0.0068 -0.0278 -0.0099 148 ARG   B C   
6227 O  O   . ARG   B 148 ? 0.1670 0.1745 0.2185 -0.0252 -0.0360 -0.0023 148 ARG   B O   
6228 C  CB  . ARG   B 148 ? 0.1473 0.1417 0.2260 -0.0028 -0.0299 -0.0163 148 ARG   B CB  
6229 C  CG  . ARG   B 148 ? 0.1476 0.1571 0.2432 -0.0087 -0.0272 -0.0318 148 ARG   B CG  
6230 C  CD  . ARG   B 148 ? 0.1521 0.1763 0.2579 0.0014  -0.0289 -0.0307 148 ARG   B CD  
6231 N  NE  . ARG   B 148 ? 0.1558 0.1720 0.2477 0.0184  -0.0328 -0.0288 148 ARG   B NE  
6232 C  CZ  . ARG   B 148 ? 0.1435 0.1649 0.2330 0.0102  -0.0244 -0.0218 148 ARG   B CZ  
6233 N  NH1 . ARG   B 148 ? 0.1397 0.1712 0.2416 -0.0036 -0.0063 -0.0187 148 ARG   B NH1 
6234 N  NH2 . ARG   B 148 ? 0.1677 0.1498 0.2277 0.0146  -0.0190 -0.0104 148 ARG   B NH2 
6248 N  N   . THR   B 149 ? 0.1499 0.1360 0.2118 -0.0061 -0.0291 0.0014  149 THR   B N   
6249 C  CA  . THR   B 149 ? 0.1584 0.1434 0.2110 -0.0113 -0.0278 0.0101  149 THR   B CA  
6250 C  C   . THR   B 149 ? 0.1561 0.1399 0.1920 -0.0142 -0.0290 0.0061  149 THR   B C   
6251 O  O   . THR   B 149 ? 0.1585 0.1382 0.2111 -0.0220 -0.0146 0.0045  149 THR   B O   
6252 C  CB  . THR   B 149 ? 0.1622 0.1361 0.2115 -0.0164 -0.0279 0.0036  149 THR   B CB  
6253 O  OG1 . THR   B 149 ? 0.1598 0.1427 0.2056 -0.0247 -0.0292 0.0020  149 THR   B OG1 
6254 C  CG2 . THR   B 149 ? 0.1684 0.1359 0.2221 -0.0067 -0.0222 0.0006  149 THR   B CG2 
6262 N  N   . ASN   B 150 ? 0.1630 0.1425 0.1894 -0.0172 -0.0343 0.0012  150 ASN   B N   
6263 C  CA  . ASN   B 150 ? 0.1716 0.1585 0.1789 -0.0216 -0.0364 -0.0004 150 ASN   B CA  
6264 C  C   . ASN   B 150 ? 0.1602 0.1464 0.1853 -0.0200 -0.0281 -0.0031 150 ASN   B C   
6265 O  O   . ASN   B 150 ? 0.1674 0.1442 0.2020 -0.0309 -0.0387 -0.0011 150 ASN   B O   
6266 C  CB  . ASN   B 150 ? 0.1906 0.1907 0.1955 -0.0304 -0.0440 0.0121  150 ASN   B CB  
6267 C  CG  . ASN   B 150 ? 0.2189 0.2332 0.2249 -0.0251 -0.0470 0.0298  150 ASN   B CG  
6268 O  OD1 . ASN   B 150 ? 0.2248 0.2490 0.2425 -0.0349 -0.0574 0.0246  150 ASN   B OD1 
6269 N  ND2 . ASN   B 150 ? 0.2287 0.2518 0.2571 -0.0154 -0.0518 0.0668  150 ASN   B ND2 
6276 N  N   . VAL   B 151 ? 0.1510 0.1440 0.1891 -0.0210 -0.0279 0.0016  151 VAL   B N   
6277 C  CA  . VAL   B 151 ? 0.1544 0.1433 0.1921 -0.0276 -0.0239 -0.0046 151 VAL   B CA  
6278 C  C   . VAL   B 151 ? 0.1578 0.1351 0.1853 -0.0313 -0.0282 -0.0023 151 VAL   B C   
6279 O  O   . VAL   B 151 ? 0.1644 0.1418 0.2182 -0.0251 -0.0201 -0.0085 151 VAL   B O   
6280 C  CB  . VAL   B 151 ? 0.1705 0.1519 0.2044 -0.0092 -0.0211 -0.0076 151 VAL   B CB  
6281 C  CG1 . VAL   B 151 ? 0.1787 0.1578 0.2272 -0.0163 -0.0092 -0.0085 151 VAL   B CG1 
6282 C  CG2 . VAL   B 151 ? 0.1872 0.1725 0.2049 0.0054  -0.0190 0.0072  151 VAL   B CG2 
6292 N  N   . TYR   B 152 ? 0.1522 0.1289 0.1815 -0.0208 -0.0247 -0.0047 152 TYR   B N   
6293 C  CA  . TYR   B 152 ? 0.1596 0.1504 0.1600 -0.0320 -0.0203 -0.0083 152 TYR   B CA  
6294 C  C   . TYR   B 152 ? 0.1588 0.1327 0.1545 -0.0232 -0.0130 -0.0166 152 TYR   B C   
6295 O  O   . TYR   B 152 ? 0.1597 0.1362 0.1767 -0.0281 -0.0133 -0.0064 152 TYR   B O   
6296 C  CB  . TYR   B 152 ? 0.1675 0.1692 0.1678 -0.0346 -0.0165 0.0050  152 TYR   B CB  
6297 C  CG  . TYR   B 152 ? 0.1849 0.1757 0.1672 -0.0428 -0.0187 0.0025  152 TYR   B CG  
6298 C  CD1 . TYR   B 152 ? 0.1972 0.1876 0.1560 -0.0354 -0.0280 0.0071  152 TYR   B CD1 
6299 C  CD2 . TYR   B 152 ? 0.2047 0.1927 0.1765 -0.0390 -0.0136 -0.0046 152 TYR   B CD2 
6300 C  CE1 . TYR   B 152 ? 0.2109 0.2061 0.1771 -0.0368 -0.0294 0.0196  152 TYR   B CE1 
6301 C  CE2 . TYR   B 152 ? 0.2161 0.2158 0.1773 -0.0475 -0.0187 -0.0073 152 TYR   B CE2 
6302 C  CZ  . TYR   B 152 ? 0.2213 0.2257 0.1679 -0.0468 -0.0399 0.0190  152 TYR   B CZ  
6303 O  OH  . TYR   B 152 ? 0.2479 0.2605 0.2112 -0.0375 -0.0442 0.0254  152 TYR   B OH  
6313 N  N   . LEU   B 153 ? 0.1606 0.1320 0.1696 -0.0306 -0.0168 -0.0071 153 LEU   B N   
6314 C  CA  . LEU   B 153 ? 0.1605 0.1316 0.1615 -0.0215 -0.0094 -0.0099 153 LEU   B CA  
6315 C  C   . LEU   B 153 ? 0.1596 0.1287 0.1733 -0.0260 -0.0079 -0.0163 153 LEU   B C   
6316 O  O   . LEU   B 153 ? 0.1693 0.1450 0.1875 -0.0151 -0.0080 -0.0303 153 LEU   B O   
6317 C  CB  . LEU   B 153 ? 0.1559 0.1252 0.1847 -0.0284 -0.0105 -0.0080 153 LEU   B CB  
6318 C  CG  . LEU   B 153 ? 0.1515 0.1403 0.2093 -0.0260 -0.0062 -0.0030 153 LEU   B CG  
6319 C  CD1 . LEU   B 153 ? 0.1643 0.1548 0.2226 -0.0265 0.0030  0.0081  153 LEU   B CD1 
6320 C  CD2 . LEU   B 153 ? 0.1515 0.1536 0.2055 -0.0299 0.0132  0.0004  153 LEU   B CD2 
6332 N  N   . ALA   B 154 ? 0.1513 0.1326 0.1859 -0.0109 -0.0157 -0.0074 154 ALA   B N   
6333 C  CA  . ALA   B 154 ? 0.1619 0.1445 0.2166 -0.0047 -0.0203 -0.0177 154 ALA   B CA  
6334 C  C   . ALA   B 154 ? 0.1733 0.1437 0.2205 -0.0015 -0.0231 -0.0235 154 ALA   B C   
6335 O  O   . ALA   B 154 ? 0.2068 0.1454 0.2289 0.0004  -0.0116 -0.0073 154 ALA   B O   
6336 C  CB  . ALA   B 154 ? 0.1596 0.1575 0.2311 -0.0054 -0.0151 -0.0294 154 ALA   B CB  
6342 N  N   . VAL   B 155 ? 0.1457 0.1334 0.2356 -0.0057 0.0011  -0.0189 155 VAL   B N   
6343 C  CA  . VAL   B 155 ? 0.1429 0.1325 0.2477 -0.0023 -0.0087 -0.0123 155 VAL   B CA  
6344 C  C   . VAL   B 155 ? 0.1399 0.1305 0.2479 -0.0058 -0.0133 -0.0194 155 VAL   B C   
6345 O  O   . VAL   B 155 ? 0.1584 0.1505 0.2890 0.0024  -0.0110 -0.0368 155 VAL   B O   
6346 C  CB  . VAL   B 155 ? 0.1471 0.1488 0.2763 -0.0059 -0.0131 0.0025  155 VAL   B CB  
6347 C  CG1 . VAL   B 155 ? 0.1561 0.1472 0.2699 -0.0111 -0.0076 -0.0078 155 VAL   B CG1 
6348 C  CG2 . VAL   B 155 ? 0.1446 0.1656 0.2954 -0.0070 -0.0115 0.0312  155 VAL   B CG2 
6358 N  N   . PHE   B 156 ? 0.1318 0.1440 0.2655 0.0011  -0.0071 -0.0199 156 PHE   B N   
6359 C  CA  . PHE   B 156 ? 0.1374 0.1502 0.3022 0.0030  -0.0046 -0.0222 156 PHE   B CA  
6360 C  C   . PHE   B 156 ? 0.1391 0.1602 0.3327 0.0132  -0.0104 -0.0380 156 PHE   B C   
6361 O  O   . PHE   B 156 ? 0.1619 0.1791 0.3602 0.0195  -0.0005 -0.0497 156 PHE   B O   
6362 C  CB  . PHE   B 156 ? 0.1468 0.1428 0.2966 0.0007  -0.0112 -0.0095 156 PHE   B CB  
6363 C  CG  . PHE   B 156 ? 0.1479 0.1626 0.3067 0.0004  -0.0087 0.0150  156 PHE   B CG  
6364 C  CD1 . PHE   B 156 ? 0.1456 0.1865 0.3350 0.0095  -0.0073 0.0432  156 PHE   B CD1 
6365 C  CD2 . PHE   B 156 ? 0.1501 0.1758 0.3095 0.0070  -0.0079 0.0229  156 PHE   B CD2 
6366 C  CE1 . PHE   B 156 ? 0.1502 0.2007 0.3467 0.0031  -0.0087 0.0423  156 PHE   B CE1 
6367 C  CE2 . PHE   B 156 ? 0.1571 0.1980 0.3306 0.0133  -0.0110 0.0207  156 PHE   B CE2 
6368 C  CZ  . PHE   B 156 ? 0.1467 0.2043 0.3500 0.0138  -0.0183 0.0270  156 PHE   B CZ  
6378 N  N   . ASP   B 157 ? 0.1396 0.1534 0.3474 0.0112  -0.0304 -0.0189 157 ASP   B N   
6379 C  CA  . ASP   B 157 ? 0.1515 0.1638 0.3880 0.0087  -0.0274 -0.0240 157 ASP   B CA  
6380 C  C   . ASP   B 157 ? 0.1534 0.1594 0.3956 0.0044  -0.0242 -0.0439 157 ASP   B C   
6381 O  O   . ASP   B 157 ? 0.1393 0.1560 0.3939 0.0039  -0.0167 -0.0374 157 ASP   B O   
6382 C  CB  . ASP   B 157 ? 0.1825 0.1837 0.3970 0.0030  -0.0513 -0.0120 157 ASP   B CB  
6383 C  CG  . ASP   B 157 ? 0.2289 0.1964 0.4223 -0.0016 -0.0399 -0.0159 157 ASP   B CG  
6384 O  OD1 . ASP   B 157 ? 0.2352 0.1861 0.4375 -0.0025 -0.0330 -0.0139 157 ASP   B OD1 
6385 O  OD2 . ASP   B 157 ? 0.2573 0.2167 0.4429 0.0005  -0.0336 -0.0171 157 ASP   B OD2 
6390 N  N   . LYS   B 158 ? 0.1572 0.1830 0.4039 0.0078  -0.0090 -0.0740 158 LYS   B N   
6391 C  CA  . LYS   B 158 ? 0.1746 0.2003 0.4068 0.0036  0.0005  -0.0972 158 LYS   B CA  
6392 C  C   . LYS   B 158 ? 0.1778 0.1837 0.4157 0.0033  -0.0052 -0.0898 158 LYS   B C   
6393 O  O   . LYS   B 158 ? 0.1763 0.1826 0.4228 -0.0074 0.0017  -0.0955 158 LYS   B O   
6394 C  CB  . LYS   B 158 ? 0.1972 0.2393 0.4096 0.0092  0.0077  -0.1156 158 LYS   B CB  
6395 C  CG  . LYS   B 158 ? 0.2349 0.2807 0.4191 0.0108  0.0115  -0.1232 158 LYS   B CG  
6396 C  CD  . LYS   B 158 ? 0.2616 0.3312 0.4318 0.0077  0.0163  -0.1170 158 LYS   B CD  
6397 C  CE  . LYS   B 158 ? 0.2790 0.3599 0.4491 0.0102  0.0152  -0.1127 158 LYS   B CE  
6398 N  NZ  . LYS   B 158 ? 0.2824 0.3816 0.4502 0.0073  0.0154  -0.1109 158 LYS   B NZ  
6412 N  N   . ASN   B 159 ? 0.1829 0.1739 0.4359 0.0043  -0.0218 -0.0679 159 ASN   B N   
6413 C  CA  . ASN   B 159 ? 0.1928 0.1713 0.4465 0.0158  -0.0383 -0.0588 159 ASN   B CA  
6414 C  C   . ASN   B 159 ? 0.1734 0.1548 0.4438 0.0116  -0.0461 -0.0487 159 ASN   B C   
6415 O  O   . ASN   B 159 ? 0.1741 0.1487 0.4657 -0.0010 -0.0510 -0.0348 159 ASN   B O   
6416 C  CB  . ASN   B 159 ? 0.2172 0.1906 0.4667 0.0202  -0.0484 -0.0578 159 ASN   B CB  
6417 C  CG  . ASN   B 159 ? 0.2410 0.2066 0.4903 0.0238  -0.0580 -0.0685 159 ASN   B CG  
6418 O  OD1 . ASN   B 159 ? 0.2507 0.2245 0.4891 0.0349  -0.0561 -0.0731 159 ASN   B OD1 
6419 N  ND2 . ASN   B 159 ? 0.2409 0.2162 0.4925 0.0227  -0.0621 -0.0603 159 ASN   B ND2 
6426 N  N   . LEU   B 160 ? 0.1604 0.1534 0.4228 0.0073  -0.0502 -0.0387 160 LEU   B N   
6427 C  CA  . LEU   B 160 ? 0.1557 0.1594 0.3864 0.0092  -0.0382 -0.0237 160 LEU   B CA  
6428 C  C   . LEU   B 160 ? 0.1517 0.1427 0.3708 0.0002  -0.0258 -0.0345 160 LEU   B C   
6429 O  O   . LEU   B 160 ? 0.1415 0.1457 0.3574 -0.0054 -0.0304 -0.0192 160 LEU   B O   
6430 C  CB  . LEU   B 160 ? 0.1527 0.1642 0.3641 0.0132  -0.0349 -0.0128 160 LEU   B CB  
6431 C  CG  . LEU   B 160 ? 0.1572 0.1801 0.3450 0.0101  -0.0313 -0.0010 160 LEU   B CG  
6432 C  CD1 . LEU   B 160 ? 0.1718 0.1982 0.3417 -0.0022 -0.0182 -0.0059 160 LEU   B CD1 
6433 C  CD2 . LEU   B 160 ? 0.1643 0.1808 0.3353 0.0255  -0.0260 -0.0123 160 LEU   B CD2 
6445 N  N   . TYR   B 161 ? 0.1505 0.1495 0.3755 -0.0074 0.0013  -0.0405 161 TYR   B N   
6446 C  CA  . TYR   B 161 ? 0.1613 0.1483 0.3575 -0.0157 0.0170  -0.0433 161 TYR   B CA  
6447 C  C   . TYR   B 161 ? 0.1676 0.1487 0.3466 -0.0160 0.0166  -0.0423 161 TYR   B C   
6448 O  O   . TYR   B 161 ? 0.1709 0.1544 0.3440 -0.0233 0.0061  -0.0336 161 TYR   B O   
6449 C  CB  . TYR   B 161 ? 0.1749 0.1561 0.3576 -0.0245 0.0337  -0.0468 161 TYR   B CB  
6450 C  CG  . TYR   B 161 ? 0.2029 0.1639 0.3409 -0.0380 0.0325  -0.0609 161 TYR   B CG  
6451 C  CD1 . TYR   B 161 ? 0.2137 0.1634 0.3363 -0.0418 0.0420  -0.0588 161 TYR   B CD1 
6452 C  CD2 . TYR   B 161 ? 0.2293 0.1760 0.3256 -0.0345 0.0254  -0.0654 161 TYR   B CD2 
6453 C  CE1 . TYR   B 161 ? 0.2385 0.1825 0.3346 -0.0481 0.0388  -0.0602 161 TYR   B CE1 
6454 C  CE2 . TYR   B 161 ? 0.2510 0.1935 0.3334 -0.0383 0.0324  -0.0634 161 TYR   B CE2 
6455 C  CZ  . TYR   B 161 ? 0.2566 0.1939 0.3334 -0.0524 0.0274  -0.0555 161 TYR   B CZ  
6456 O  OH  . TYR   B 161 ? 0.2884 0.2172 0.3503 -0.0486 0.0299  -0.0520 161 TYR   B OH  
6466 N  N   . ASP   B 162 ? 0.1748 0.1461 0.3609 -0.0151 0.0071  -0.0587 162 ASP   B N   
6467 C  CA  . ASP   B 162 ? 0.1793 0.1507 0.3725 -0.0061 0.0011  -0.0548 162 ASP   B CA  
6468 C  C   . ASP   B 162 ? 0.1743 0.1429 0.3675 -0.0086 -0.0036 -0.0419 162 ASP   B C   
6469 O  O   . ASP   B 162 ? 0.1796 0.1518 0.3676 -0.0182 -0.0210 -0.0307 162 ASP   B O   
6470 C  CB  . ASP   B 162 ? 0.1976 0.1671 0.3898 -0.0024 -0.0099 -0.0765 162 ASP   B CB  
6471 C  CG  . ASP   B 162 ? 0.2059 0.2000 0.4160 0.0106  -0.0117 -0.0883 162 ASP   B CG  
6472 O  OD1 . ASP   B 162 ? 0.2060 0.2162 0.4145 0.0025  0.0062  -0.0779 162 ASP   B OD1 
6473 O  OD2 . ASP   B 162 ? 0.2171 0.2235 0.4399 0.0270  -0.0117 -0.0894 162 ASP   B OD2 
6478 N  N   . LYS   B 163 ? 0.1722 0.1317 0.3638 -0.0064 -0.0191 -0.0220 163 LYS   B N   
6479 C  CA  . LYS   B 163 ? 0.1843 0.1426 0.3597 -0.0223 -0.0131 -0.0111 163 LYS   B CA  
6480 C  C   . LYS   B 163 ? 0.1547 0.1386 0.3379 -0.0194 -0.0163 0.0017  163 LYS   B C   
6481 O  O   . LYS   B 163 ? 0.1520 0.1500 0.3548 -0.0191 -0.0161 0.0003  163 LYS   B O   
6482 C  CB  . LYS   B 163 ? 0.2268 0.1842 0.3974 -0.0233 -0.0180 -0.0010 163 LYS   B CB  
6483 C  CG  . LYS   B 163 ? 0.3038 0.2665 0.4473 -0.0257 -0.0082 0.0054  163 LYS   B CG  
6484 C  CD  . LYS   B 163 ? 0.3663 0.3467 0.5016 -0.0346 -0.0077 0.0003  163 LYS   B CD  
6485 C  CE  . LYS   B 163 ? 0.4203 0.3988 0.5361 -0.0397 -0.0013 -0.0015 163 LYS   B CE  
6486 N  NZ  . LYS   B 163 ? 0.4504 0.4404 0.5594 -0.0424 0.0010  -0.0068 163 LYS   B NZ  
6500 N  N   . LEU   B 164 ? 0.1403 0.1332 0.3198 -0.0172 -0.0180 -0.0059 164 LEU   B N   
6501 C  CA  . LEU   B 164 ? 0.1457 0.1336 0.3093 -0.0151 -0.0283 0.0018  164 LEU   B CA  
6502 C  C   . LEU   B 164 ? 0.1546 0.1332 0.3130 -0.0159 -0.0389 0.0033  164 LEU   B C   
6503 O  O   . LEU   B 164 ? 0.1586 0.1559 0.3259 -0.0176 -0.0358 0.0007  164 LEU   B O   
6504 C  CB  . LEU   B 164 ? 0.1396 0.1348 0.2907 -0.0124 -0.0229 0.0028  164 LEU   B CB  
6505 C  CG  . LEU   B 164 ? 0.1488 0.1518 0.2887 -0.0090 -0.0131 0.0126  164 LEU   B CG  
6506 C  CD1 . LEU   B 164 ? 0.1497 0.1486 0.2733 -0.0163 -0.0196 0.0014  164 LEU   B CD1 
6507 C  CD2 . LEU   B 164 ? 0.1628 0.1867 0.3082 -0.0061 -0.0041 0.0035  164 LEU   B CD2 
6519 N  N   . VAL   B 165 ? 0.1878 0.1463 0.3256 -0.0245 -0.0428 -0.0044 165 VAL   B N   
6520 C  CA  . VAL   B 165 ? 0.2246 0.1559 0.3268 -0.0347 -0.0564 -0.0053 165 VAL   B CA  
6521 C  C   . VAL   B 165 ? 0.2515 0.1648 0.3607 -0.0436 -0.0819 -0.0063 165 VAL   B C   
6522 O  O   . VAL   B 165 ? 0.2752 0.1816 0.3729 -0.0477 -0.0841 0.0056  165 VAL   B O   
6523 C  CB  . VAL   B 165 ? 0.2491 0.1700 0.3264 -0.0200 -0.0288 -0.0133 165 VAL   B CB  
6524 C  CG1 . VAL   B 165 ? 0.2643 0.1815 0.3457 -0.0171 -0.0151 -0.0073 165 VAL   B CG1 
6525 C  CG2 . VAL   B 165 ? 0.2480 0.1751 0.3173 -0.0137 -0.0212 -0.0105 165 VAL   B CG2 
6535 N  N   . SER   B 166 ? 0.2589 0.1553 0.3886 -0.0380 -0.0952 -0.0312 166 SER   B N   
6536 C  CA  . SER   B 166 ? 0.2545 0.1612 0.4346 -0.0342 -0.0843 -0.0325 166 SER   B CA  
6537 C  C   . SER   B 166 ? 0.2376 0.1757 0.4430 -0.0396 -0.0819 -0.0115 166 SER   B C   
6538 O  O   . SER   B 166 ? 0.2410 0.1972 0.4617 -0.0513 -0.0876 -0.0369 166 SER   B O   
6539 C  CB  . SER   B 166 ? 0.2577 0.1711 0.4599 -0.0281 -0.0766 -0.0423 166 SER   B CB  
6540 O  OG  . SER   B 166 ? 0.2441 0.1682 0.4747 -0.0194 -0.0783 -0.0292 166 SER   B OG  
6546 N  N   . SER   B 167 ? 0.2150 0.1643 0.4206 -0.0455 -0.0856 0.0229  167 SER   B N   
6547 C  CA  . SER   B 167 ? 0.2087 0.1722 0.4042 -0.0384 -0.0593 0.0270  167 SER   B CA  
6548 C  C   . SER   B 167 ? 0.2043 0.1770 0.3833 -0.0507 -0.0498 0.0443  167 SER   B C   
6549 O  O   . SER   B 167 ? 0.2040 0.1917 0.3777 -0.0539 -0.0499 0.0449  167 SER   B O   
6550 C  CB  . SER   B 167 ? 0.1964 0.1781 0.4075 -0.0330 -0.0286 0.0205  167 SER   B CB  
6551 O  OG  . SER   B 167 ? 0.1876 0.1860 0.4039 -0.0231 -0.0034 0.0222  167 SER   B OG  
6557 N  N   . PHE   B 168 ? 0.2020 0.1760 0.3743 -0.0437 -0.0378 0.0506  168 PHE   B N   
6558 C  CA  . PHE   B 168 ? 0.2044 0.1746 0.3354 -0.0448 -0.0345 0.0311  168 PHE   B CA  
6559 C  C   . PHE   B 168 ? 0.1773 0.1579 0.2965 -0.0271 -0.0167 0.0127  168 PHE   B C   
6560 O  O   . PHE   B 168 ? 0.2087 0.1548 0.2944 -0.0017 -0.0178 0.0021  168 PHE   B O   
6561 C  CB  . PHE   B 168 ? 0.2233 0.1783 0.3365 -0.0587 -0.0456 0.0422  168 PHE   B CB  
6562 C  CG  . PHE   B 168 ? 0.2494 0.1597 0.3199 -0.0619 -0.0480 0.0208  168 PHE   B CG  
6563 C  CD1 . PHE   B 168 ? 0.2806 0.1626 0.3215 -0.0536 -0.0483 0.0183  168 PHE   B CD1 
6564 C  CD2 . PHE   B 168 ? 0.2420 0.1564 0.3136 -0.0582 -0.0432 0.0293  168 PHE   B CD2 
6565 C  CE1 . PHE   B 168 ? 0.2889 0.1739 0.3196 -0.0422 -0.0413 0.0256  168 PHE   B CE1 
6566 C  CE2 . PHE   B 168 ? 0.2699 0.1628 0.3137 -0.0407 -0.0490 0.0242  168 PHE   B CE2 
6567 C  CZ  . PHE   B 168 ? 0.2814 0.1621 0.3124 -0.0300 -0.0534 0.0342  168 PHE   B CZ  
6577 N  N   . LEU   B 169 ? 0.1795 0.1680 0.2885 -0.0065 -0.0022 -0.0008 169 LEU   B N   
6578 C  CA  . LEU   B 169 ? 0.2056 0.1989 0.3145 -0.0044 0.0043  -0.0266 169 LEU   B CA  
6579 C  C   . LEU   B 169 ? 0.2388 0.2257 0.3649 0.0084  -0.0034 -0.0489 169 LEU   B C   
6580 O  O   . LEU   B 169 ? 0.2603 0.2493 0.4125 0.0067  -0.0062 -0.0645 169 LEU   B O   
6581 C  CB  . LEU   B 169 ? 0.2253 0.2405 0.3221 -0.0122 0.0033  -0.0026 169 LEU   B CB  
6582 C  CG  . LEU   B 169 ? 0.2623 0.2792 0.3503 -0.0038 0.0071  0.0033  169 LEU   B CG  
6583 C  CD1 . LEU   B 169 ? 0.2771 0.2976 0.3527 -0.0047 0.0042  0.0215  169 LEU   B CD1 
6584 C  CD2 . LEU   B 169 ? 0.2537 0.2853 0.3449 0.0078  0.0243  -0.0124 169 LEU   B CD2 
6585 O  OXT . LEU   B 169 ? 0.2580 0.2395 0.3748 0.0301  -0.0005 -0.0488 169 LEU   B OXT 
6597 C  C1  T TFA   C .   ? 0.1359 0.1557 0.1234 -0.0157 0.0187  0.0140  201 TFA   A C1  
6598 C  C2  T TFA   C .   ? 0.1618 0.1780 0.1627 -0.0226 0.0171  -0.0014 201 TFA   A C2  
6599 O  O   T TFA   C .   ? 0.1143 0.1326 0.1145 -0.0159 0.0166  0.0322  201 TFA   A O   
6600 F  F1  T TFA   C .   ? 0.1720 0.1782 0.1974 -0.0226 0.0119  -0.0135 201 TFA   A F1  
6601 F  F2  T TFA   C .   ? 0.1760 0.1935 0.1596 -0.0227 0.0251  0.0097  201 TFA   A F2  
6602 F  F3  T TFA   C .   ? 0.1685 0.1923 0.1817 -0.0294 0.0290  -0.0083 201 TFA   A F3  
6603 O  OXT T TFA   C .   ? 0.1345 0.1566 0.1332 0.0062  0.0223  0.0153  201 TFA   A OXT 
6604 N  N2  B A1A6Y D .   ? 0.1563 0.1574 0.1796 -0.0077 0.0017  0.0163  202 A1A6Y A N2  
6605 C  C3  B A1A6Y D .   ? 0.1911 0.1857 0.2082 -0.0043 0.0035  0.0127  202 A1A6Y A C3  
6606 C  C6  B A1A6Y D .   ? 0.2165 0.1938 0.2260 0.0005  0.0086  0.0266  202 A1A6Y A C6  
6607 C  C9  B A1A6Y D .   ? 0.1263 0.1501 0.1799 -0.0014 -0.0127 0.0223  202 A1A6Y A C9  
6608 C  C12 B A1A6Y D .   ? 0.1071 0.1483 0.1720 -0.0047 -0.0189 0.0281  202 A1A6Y A C12 
6609 C  C1  B A1A6Y D .   ? 0.1792 0.1808 0.2071 -0.0115 0.0148  -0.0021 202 A1A6Y A C1  
6610 C  C10 B A1A6Y D .   ? 0.1290 0.1560 0.1818 -0.0051 -0.0088 0.0199  202 A1A6Y A C10 
6611 C  C11 B A1A6Y D .   ? 0.1154 0.1559 0.1772 -0.0012 -0.0088 0.0233  202 A1A6Y A C11 
6612 C  C2  B A1A6Y D .   ? 0.1756 0.1734 0.1973 -0.0095 0.0085  0.0100  202 A1A6Y A C2  
6613 C  C4  B A1A6Y D .   ? 0.2043 0.1891 0.2235 0.0005  0.0035  0.0213  202 A1A6Y A C4  
6614 C  C5  B A1A6Y D .   ? 0.2112 0.1955 0.2204 -0.0004 0.0037  0.0206  202 A1A6Y A C5  
6615 C  C7  B A1A6Y D .   ? 0.1455 0.1602 0.1862 -0.0085 -0.0052 0.0140  202 A1A6Y A C7  
6616 C  C8  B A1A6Y D .   ? 0.1458 0.1628 0.1933 -0.0038 -0.0051 0.0182  202 A1A6Y A C8  
6617 N  N1  B A1A6Y D .   ? 0.2191 0.1943 0.2238 -0.0003 0.0057  0.0213  202 A1A6Y A N1  
6618 N  N3  B A1A6Y D .   ? 0.1486 0.1623 0.2002 -0.0090 -0.0046 0.0072  202 A1A6Y A N3  
6619 N  N4  B A1A6Y D .   ? 0.1408 0.1600 0.1866 -0.0043 -0.0075 0.0232  202 A1A6Y A N4  
6620 N  N5  B A1A6Y D .   ? 0.1109 0.1401 0.1672 0.0016  -0.0194 0.0330  202 A1A6Y A N5  
6621 O  O1  B A1A6Y D .   ? 0.1796 0.1866 0.2125 -0.0123 0.0145  -0.0040 202 A1A6Y A O1  
6622 S  S1  B A1A6Y D .   ? 0.2109 0.1848 0.2414 0.0091  0.0036  0.0268  202 A1A6Y A S1  
6636 CL CL  B CL    E .   ? 0.1684 0.1514 0.2957 -0.0200 -0.0009 0.0374  203 CL    A CL  
6637 O  O   . HOH   F .   ? 0.1555 0.4514 0.2492 0.0080  0.0309  0.0707  301 HOH   A O   
6638 O  O   . HOH   F .   ? 0.4073 0.8124 0.4840 -0.1049 0.0369  0.1134  302 HOH   A O   
6639 O  O   . HOH   F .   ? 0.7292 0.5496 0.4496 -0.1564 -0.0573 0.1902  303 HOH   A O   
6640 O  O   . HOH   F .   ? 0.2950 0.2643 0.4417 -0.0480 -0.1253 0.1149  304 HOH   A O   
6641 O  O   . HOH   F .   ? 0.2900 0.5991 0.5905 -0.0552 -0.0915 0.2124  305 HOH   A O   
6642 O  O   . HOH   F .   ? 0.6030 0.4783 0.3290 0.1926  -0.1123 0.0560  306 HOH   A O   
6643 O  O   B HOH   F .   ? 0.3871 0.6262 0.3771 0.1514  0.0222  0.0512  307 HOH   A O   
6644 O  O   A HOH   F .   ? 0.2383 0.2134 0.3649 -0.0218 -0.0258 0.0297  308 HOH   A O   
6645 O  O   . HOH   F .   ? 0.4371 0.3472 0.4475 -0.0210 0.1018  -0.0127 309 HOH   A O   
6646 O  O   . HOH   F .   ? 0.5699 0.4672 0.4594 -0.0506 0.1440  0.1964  310 HOH   A O   
6647 O  O   . HOH   F .   ? 0.5767 0.3646 0.5396 -0.0705 0.1646  0.1100  311 HOH   A O   
6648 O  O   B HOH   F .   ? 0.1718 0.2605 0.2908 -0.0641 0.0244  -0.0014 312 HOH   A O   
6649 O  O   . HOH   F .   ? 0.3025 0.3521 0.1904 -0.0501 0.0415  0.0551  313 HOH   A O   
6650 O  O   . HOH   F .   ? 0.5249 0.6771 0.5011 -0.1226 -0.1170 -0.0993 314 HOH   A O   
6651 O  O   . HOH   F .   ? 0.3625 0.3427 0.3129 -0.1302 0.0124  0.0970  315 HOH   A O   
6652 O  O   . HOH   F .   ? 0.5129 0.2680 0.3129 -0.1293 0.0478  0.0362  316 HOH   A O   
6653 O  O   . HOH   F .   ? 0.6038 0.3416 0.3483 -0.0757 -0.0471 0.0130  317 HOH   A O   
6654 O  O   . HOH   F .   ? 0.2210 0.1870 0.3751 -0.0502 0.0059  -0.0195 318 HOH   A O   
6655 O  O   . HOH   F .   ? 0.1797 0.4537 0.3151 0.0837  0.0078  0.0560  319 HOH   A O   
6656 O  O   . HOH   F .   ? 0.4481 0.4860 0.3494 0.1697  -0.0880 -0.1578 320 HOH   A O   
6657 O  O   . HOH   F .   ? 0.2208 0.1762 0.2755 -0.0031 -0.0653 -0.0102 321 HOH   A O   
6658 O  O   B HOH   F .   ? 0.2338 0.3183 0.2129 0.1467  0.0035  0.0616  322 HOH   A O   
6659 O  O   . HOH   F .   ? 0.6354 0.4536 0.5616 0.0669  -0.0597 -0.0258 323 HOH   A O   
6660 O  O   . HOH   F .   ? 0.1591 0.1803 0.2888 0.0056  -0.0355 -0.0515 324 HOH   A O   
6661 O  O   A HOH   F .   ? 0.2185 0.3038 0.4078 0.0153  0.0876  0.1599  325 HOH   A O   
6662 O  O   . HOH   F .   ? 0.2019 0.3852 0.3787 -0.0359 0.0409  -0.1120 326 HOH   A O   
6663 O  O   A HOH   F .   ? 0.2011 0.2166 0.2297 -0.0338 0.0326  0.0451  327 HOH   A O   
6664 O  O   . HOH   F .   ? 0.1606 0.1527 0.2396 -0.0206 0.0079  0.0111  328 HOH   A O   
6665 O  O   . HOH   F .   ? 0.4487 0.4949 0.6542 0.1600  0.1384  -0.1121 329 HOH   A O   
6666 O  O   . HOH   F .   ? 0.6823 0.5504 0.3735 -0.0798 -0.0127 0.1088  330 HOH   A O   
6667 O  O   . HOH   F .   ? 0.3255 0.4652 0.2496 -0.0123 0.0531  0.0417  331 HOH   A O   
6668 O  O   . HOH   F .   ? 0.1756 0.1681 0.2240 0.0132  -0.0297 0.0260  332 HOH   A O   
6669 O  O   . HOH   F .   ? 0.4263 0.3996 0.3845 -0.0581 0.1972  0.0641  333 HOH   A O   
6670 O  O   . HOH   F .   ? 0.6598 0.6537 0.4536 -0.0153 -0.0712 -0.0871 334 HOH   A O   
6671 O  O   . HOH   F .   ? 0.4888 0.5707 0.2981 -0.1117 0.1286  0.0914  335 HOH   A O   
6672 O  O   . HOH   F .   ? 0.2927 0.5967 0.6366 0.1336  0.0915  0.1548  336 HOH   A O   
6673 O  O   B HOH   F .   ? 0.3541 0.2940 0.3210 -0.0582 -0.0005 0.0656  337 HOH   A O   
6674 O  O   . HOH   F .   ? 0.2047 0.4570 0.4246 -0.0217 -0.0551 0.2077  338 HOH   A O   
6675 O  O   A HOH   F .   ? 0.1428 0.2199 0.2080 0.0478  0.0331  0.0532  339 HOH   A O   
6676 O  O   . HOH   F .   ? 0.2665 0.5613 0.3886 0.0188  -0.0384 0.0805  340 HOH   A O   
6677 O  O   . HOH   F .   ? 0.3333 0.2825 0.3304 -0.0828 0.0009  -0.0159 341 HOH   A O   
6678 O  O   B HOH   F .   ? 0.2968 0.3294 0.1617 -0.0137 -0.0071 0.0613  342 HOH   A O   
6679 O  O   . HOH   F .   ? 0.2397 0.2339 0.3008 0.0377  0.0276  0.0544  343 HOH   A O   
6680 O  O   . HOH   F .   ? 0.2340 0.4115 0.3514 0.0880  -0.0575 -0.0125 344 HOH   A O   
6681 O  O   . HOH   F .   ? 0.4790 0.1991 0.4894 0.0502  -0.1638 0.0509  345 HOH   A O   
6682 O  O   . HOH   F .   ? 0.2023 0.1648 0.1760 -0.0102 0.0150  0.0201  346 HOH   A O   
6683 O  O   . HOH   F .   ? 0.6150 0.5672 0.5065 0.0751  0.2382  -0.0917 347 HOH   A O   
6684 O  O   . HOH   F .   ? 0.5049 0.4488 0.4586 -0.1903 -0.0758 0.2228  348 HOH   A O   
6685 O  O   . HOH   F .   ? 0.2730 0.3576 0.3746 -0.0859 -0.0519 -0.0429 349 HOH   A O   
6686 O  O   . HOH   F .   ? 0.2614 0.2140 0.2468 -0.0363 0.0257  -0.0090 350 HOH   A O   
6687 O  O   . HOH   F .   ? 0.5011 0.2003 0.5059 0.0584  0.0546  0.0150  351 HOH   A O   
6688 O  O   . HOH   F .   ? 0.1936 0.1978 0.4616 0.0142  0.1075  -0.0195 352 HOH   A O   
6689 O  O   . HOH   F .   ? 0.2163 0.1693 0.2481 0.0278  -0.0322 -0.0036 353 HOH   A O   
6690 O  O   . HOH   F .   ? 0.1431 0.2107 0.2255 0.0016  -0.0142 0.0392  354 HOH   A O   
6691 O  O   . HOH   F .   ? 0.4006 0.4358 0.4078 0.2023  0.0867  0.0418  355 HOH   A O   
6692 O  O   B HOH   F .   ? 0.2901 0.1993 0.2504 0.0361  -0.0431 -0.0033 356 HOH   A O   
6693 O  O   . HOH   F .   ? 0.3544 0.6128 0.5459 0.0042  -0.0256 0.2086  357 HOH   A O   
6694 O  O   A HOH   F .   ? 0.1880 0.2879 0.2131 0.0386  0.0174  0.0263  358 HOH   A O   
6695 O  O   . HOH   F .   ? 0.3841 0.3305 0.2361 -0.0671 -0.0195 0.0181  359 HOH   A O   
6696 O  O   . HOH   F .   ? 0.1370 0.1274 0.1553 -0.0040 0.0142  0.0104  360 HOH   A O   
6697 O  O   . HOH   F .   ? 0.3075 0.3363 0.4937 -0.0701 -0.1010 -0.0765 361 HOH   A O   
6698 O  O   A HOH   F .   ? 0.6193 0.2764 0.4925 -0.0304 -0.1228 0.0996  362 HOH   A O   
6699 O  O   . HOH   F .   ? 0.1502 0.1990 0.2663 0.0028  -0.0050 0.0122  363 HOH   A O   
6700 O  O   . HOH   F .   ? 0.2599 0.4155 0.3380 -0.0585 0.0686  0.0093  364 HOH   A O   
6701 O  O   B HOH   F .   ? 0.2358 0.1786 0.2300 0.0216  -0.0148 -0.0084 365 HOH   A O   
6702 O  O   . HOH   F .   ? 0.5799 0.4136 0.6003 0.1212  0.2095  -0.1328 366 HOH   A O   
6703 O  O   . HOH   F .   ? 0.3281 0.3790 0.2288 -0.1029 -0.0192 -0.0766 367 HOH   A O   
6704 O  O   . HOH   F .   ? 0.1573 0.1366 0.2603 -0.0102 0.0177  -0.0136 368 HOH   A O   
6705 O  O   . HOH   F .   ? 0.6201 0.4172 0.3621 0.0287  -0.0042 0.1734  369 HOH   A O   
6706 O  O   . HOH   F .   ? 0.2774 0.4634 0.3189 0.0807  0.0918  0.1944  370 HOH   A O   
6707 O  O   A HOH   F .   ? 0.3260 0.1594 0.2087 0.0159  0.0252  0.0016  371 HOH   A O   
6708 O  O   . HOH   F .   ? 0.1447 0.1547 0.1697 -0.0051 -0.0158 -0.0019 372 HOH   A O   
6709 O  O   A HOH   F .   ? 0.2702 0.2364 0.2332 0.0654  0.0442  0.0497  373 HOH   A O   
6710 O  O   B HOH   F .   ? 0.1306 0.1929 0.1320 -0.0443 -0.0169 0.0173  374 HOH   A O   
6711 O  O   . HOH   F .   ? 0.3986 0.2419 0.4511 -0.1141 0.0854  0.0387  375 HOH   A O   
6712 O  O   . HOH   F .   ? 0.3984 0.2093 0.2452 0.1159  0.0469  0.0253  376 HOH   A O   
6713 O  O   . HOH   F .   ? 0.3027 0.4378 0.3779 -0.0468 -0.0392 0.1106  377 HOH   A O   
6714 O  O   . HOH   F .   ? 0.4370 0.2450 0.4165 -0.1363 0.1588  -0.0279 378 HOH   A O   
6715 O  O   . HOH   F .   ? 0.1868 0.1906 0.2634 -0.0290 0.0080  0.0340  379 HOH   A O   
6716 O  O   . HOH   F .   ? 0.3700 0.7159 0.5157 -0.0586 -0.1411 0.0624  380 HOH   A O   
6717 O  O   . HOH   F .   ? 0.1748 0.2248 0.2059 -0.0212 -0.0054 0.0679  381 HOH   A O   
6718 O  O   . HOH   F .   ? 0.1966 0.2378 0.2522 -0.0353 -0.0484 0.0605  382 HOH   A O   
6719 O  O   . HOH   F .   ? 0.2012 0.2487 0.3542 0.0118  0.0830  -0.0614 383 HOH   A O   
6720 O  O   . HOH   F .   ? 0.3014 0.6782 0.3383 0.1287  0.0578  -0.0475 384 HOH   A O   
6721 O  O   . HOH   F .   ? 0.3151 0.2451 0.5128 -0.0785 -0.0328 0.0358  385 HOH   A O   
6722 O  O   . HOH   F .   ? 0.2944 0.3068 0.2281 0.0273  0.0685  0.0181  386 HOH   A O   
6723 O  O   T HOH   F .   ? 0.1016 0.1033 0.2452 -0.0238 0.0123  0.0355  387 HOH   A O   
6724 O  O   . HOH   F .   ? 0.1840 0.2821 0.2831 0.0397  0.0376  0.0973  388 HOH   A O   
6725 O  O   . HOH   F .   ? 0.3368 0.2556 0.3272 -0.0118 -0.0415 0.0891  389 HOH   A O   
6726 O  O   B HOH   F .   ? 0.1927 0.1993 0.3044 0.0191  -0.0293 0.0218  390 HOH   A O   
6727 O  O   . HOH   F .   ? 0.2041 0.2114 0.3905 -0.0063 -0.0530 0.0359  391 HOH   A O   
6728 O  O   . HOH   F .   ? 0.1919 0.1869 0.1977 0.0093  0.0105  0.0206  392 HOH   A O   
6729 O  O   . HOH   F .   ? 0.1709 0.1683 0.2483 -0.0172 0.0141  0.0297  393 HOH   A O   
6730 O  O   . HOH   F .   ? 0.3144 0.4159 0.4300 -0.0857 0.1452  -0.0474 394 HOH   A O   
6731 O  O   . HOH   F .   ? 0.1920 0.2173 0.3038 -0.0182 -0.0315 0.0808  395 HOH   A O   
6732 O  O   . HOH   F .   ? 0.2456 0.2027 0.1932 -0.0546 0.0042  0.0368  396 HOH   A O   
6733 O  O   . HOH   F .   ? 0.1880 0.1910 0.3997 0.0384  0.1044  0.1021  397 HOH   A O   
6734 O  O   . HOH   F .   ? 0.2903 0.3635 0.3600 -0.1249 0.0778  -0.0048 398 HOH   A O   
6735 O  O   . HOH   F .   ? 0.5870 0.2914 0.5500 0.1014  -0.0526 -0.0165 399 HOH   A O   
6736 O  O   . HOH   F .   ? 0.1466 0.1609 0.1975 0.0085  -0.0261 -0.0236 400 HOH   A O   
6737 O  O   . HOH   F .   ? 0.2523 0.3990 0.3922 -0.0362 0.1099  -0.1050 401 HOH   A O   
6738 O  O   . HOH   F .   ? 0.3122 0.4226 0.2149 -0.0771 -0.0638 0.0344  402 HOH   A O   
6739 O  O   . HOH   F .   ? 0.5821 0.5607 0.6874 -0.0905 0.0263  0.1735  403 HOH   A O   
6740 O  O   . HOH   F .   ? 0.6565 0.3391 0.5411 0.0395  0.0927  0.1591  404 HOH   A O   
6741 O  O   . HOH   F .   ? 0.3071 0.2779 0.2544 -0.0848 -0.1005 0.0442  405 HOH   A O   
6742 O  O   . HOH   F .   ? 0.2449 0.1764 0.2800 -0.0041 0.0064  0.0290  406 HOH   A O   
6743 O  O   . HOH   F .   ? 0.2542 0.2872 0.3515 -0.0151 -0.0247 -0.0708 407 HOH   A O   
6744 O  O   . HOH   F .   ? 0.3619 0.6333 0.4244 -0.0797 -0.0212 0.1577  408 HOH   A O   
6745 O  O   . HOH   F .   ? 0.1327 0.1447 0.2028 -0.0044 -0.0121 0.0086  409 HOH   A O   
6746 O  O   . HOH   F .   ? 0.6170 0.6130 0.4163 0.2071  -0.0570 -0.0299 410 HOH   A O   
6747 O  O   . HOH   F .   ? 0.2209 0.1727 0.3098 0.0082  -0.0307 0.0101  411 HOH   A O   
6748 O  O   . HOH   F .   ? 0.5332 0.4716 0.2047 -0.0346 0.0873  0.0756  412 HOH   A O   
6749 O  O   . HOH   F .   ? 0.1513 0.1649 0.3213 -0.0008 0.0005  0.0270  413 HOH   A O   
6750 O  O   . HOH   F .   ? 0.4261 0.6647 0.5649 0.1963  0.1077  0.0473  414 HOH   A O   
6751 O  O   . HOH   F .   ? 0.1853 0.2585 0.3953 -0.0054 -0.0207 0.0232  415 HOH   A O   
6752 O  O   . HOH   F .   ? 0.1780 0.1415 0.1672 -0.0260 0.0098  0.0053  416 HOH   A O   
6753 O  O   . HOH   F .   ? 0.2948 0.3778 0.7296 -0.0328 0.1330  -0.0527 417 HOH   A O   
6754 O  O   A HOH   F .   ? 0.1926 0.1762 0.3265 -0.0140 0.0285  -0.0031 418 HOH   A O   
6755 O  O   . HOH   F .   ? 0.2426 0.2111 0.2729 -0.0578 -0.0053 0.0627  419 HOH   A O   
6756 O  O   . HOH   F .   ? 0.2058 0.2982 0.2735 -0.0217 -0.0578 0.0594  420 HOH   A O   
6757 O  O   . HOH   F .   ? 0.2780 0.6586 0.1935 -0.0309 0.0511  0.0148  421 HOH   A O   
6758 O  O   A HOH   F .   ? 0.2143 0.2105 0.2521 0.0106  -0.0055 0.0513  422 HOH   A O   
6759 O  O   . HOH   F .   ? 0.3381 0.1347 0.2158 -0.0009 -0.0547 0.0126  423 HOH   A O   
6760 O  O   A HOH   F .   ? 0.1891 0.2193 0.3306 0.0048  -0.0344 -0.0560 424 HOH   A O   
6761 O  O   . HOH   F .   ? 0.2472 0.4359 0.2823 0.1709  0.0065  0.0451  425 HOH   A O   
6762 O  O   . HOH   F .   ? 0.4237 0.2270 0.5712 -0.0877 -0.2269 0.0983  426 HOH   A O   
6763 O  O   A HOH   F .   ? 0.2530 0.2649 0.2502 -0.0213 0.0809  -0.0075 427 HOH   A O   
6764 O  O   . HOH   F .   ? 0.4420 0.6386 0.3336 -0.0883 -0.0038 0.1585  428 HOH   A O   
6765 O  O   . HOH   F .   ? 0.1632 0.1987 0.2888 -0.0133 0.0078  0.0373  429 HOH   A O   
6766 O  O   . HOH   F .   ? 0.6669 0.4166 0.4802 0.1853  -0.0878 0.1601  430 HOH   A O   
6767 O  O   A HOH   F .   ? 0.1468 0.2340 0.2823 -0.0268 0.0586  0.0443  431 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2055 0.1874 0.3275 0.0244  -0.0640 0.0146  432 HOH   A O   
6769 O  O   A HOH   F .   ? 0.6444 0.5005 0.4786 -0.1043 0.1061  0.1514  433 HOH   A O   
6770 O  O   . HOH   F .   ? 0.4337 0.4715 0.4271 0.2010  0.0516  -0.0452 434 HOH   A O   
6771 O  O   . HOH   F .   ? 0.5918 0.6530 0.6664 -0.1312 -0.0905 -0.0487 435 HOH   A O   
6772 O  O   A HOH   F .   ? 0.1679 0.1416 0.2202 -0.0012 -0.0244 0.0167  436 HOH   A O   
6773 O  O   . HOH   F .   ? 0.6191 0.7330 0.5719 -0.0932 0.0921  0.0248  437 HOH   A O   
6774 O  O   . HOH   F .   ? 0.6483 0.7210 0.4634 0.0879  0.2736  -0.0548 438 HOH   A O   
6775 O  O   . HOH   F .   ? 0.9054 0.9826 0.7459 0.0174  -0.0213 -0.0099 439 HOH   A O   
6776 O  O   . HOH   F .   ? 0.3376 0.2944 0.1973 -0.0818 0.0193  0.0650  440 HOH   A O   
6777 O  O   . HOH   F .   ? 0.5455 0.4839 0.3935 -0.0296 -0.1589 0.0364  441 HOH   A O   
6778 O  O   . HOH   F .   ? 0.2552 0.1624 0.3013 0.0085  0.0046  0.0084  442 HOH   A O   
6779 O  O   A HOH   F .   ? 0.2420 0.1577 0.2176 -0.0200 -0.0324 -0.0052 443 HOH   A O   
6780 O  O   . HOH   F .   ? 0.1919 0.2275 0.4849 -0.0236 -0.0883 0.0638  444 HOH   A O   
6781 O  O   . HOH   F .   ? 0.5897 0.6264 0.6564 -0.1418 -0.0050 -0.1276 445 HOH   A O   
6782 O  O   . HOH   F .   ? 0.4607 0.4603 0.4869 -0.1183 -0.0978 -0.1294 446 HOH   A O   
6783 O  O   . HOH   F .   ? 0.1788 0.1657 0.1702 -0.0110 -0.0152 -0.0023 447 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3652 0.3363 0.3384 0.1916  -0.0690 -0.0465 448 HOH   A O   
6785 O  O   . HOH   F .   ? 0.6059 0.7772 0.4404 0.1685  -0.0931 0.2428  449 HOH   A O   
6786 O  O   A HOH   F .   ? 0.5817 0.2572 0.5798 0.0493  0.0981  -0.0762 450 HOH   A O   
6787 O  O   . HOH   F .   ? 0.2839 0.3391 0.5608 0.0017  0.0964  -0.1478 451 HOH   A O   
6788 O  O   . HOH   F .   ? 0.2112 0.2784 0.2706 -0.0057 -0.0170 -0.0480 452 HOH   A O   
6789 O  O   A HOH   F .   ? 0.6098 0.3115 0.3411 -0.0572 0.0957  0.1137  453 HOH   A O   
6790 O  O   . HOH   F .   ? 0.7018 0.5786 0.7364 0.1207  -0.0980 0.2014  454 HOH   A O   
6791 O  O   . HOH   F .   ? 0.6777 0.6984 0.6407 0.0770  -0.1076 -0.0034 455 HOH   A O   
6792 O  O   . HOH   F .   ? 0.2147 0.2071 0.2951 0.0065  0.0245  0.0241  456 HOH   A O   
6793 O  O   . HOH   F .   ? 0.4592 0.5602 0.4354 0.0425  0.0147  0.0817  457 HOH   A O   
6794 O  O   . HOH   F .   ? 0.6419 0.6060 0.4867 -0.0383 0.1105  0.1616  458 HOH   A O   
6795 O  O   . HOH   F .   ? 0.5401 0.3675 0.4122 -0.0147 0.0092  0.0666  459 HOH   A O   
6796 O  O   . HOH   F .   ? 0.5760 0.6973 0.5497 0.1416  0.0475  0.0326  460 HOH   A O   
6797 O  O   B HOH   F .   ? 0.2834 0.1955 0.3166 0.0107  0.0281  0.0271  461 HOH   A O   
6798 O  O   . HOH   F .   ? 0.3436 0.4513 0.3981 0.1847  -0.0145 0.0947  462 HOH   A O   
6799 O  O   . HOH   F .   ? 0.4308 0.3035 0.4440 0.0506  0.1060  0.0308  463 HOH   A O   
6800 O  O   B HOH   F .   ? 0.3037 0.1774 0.3535 -0.0408 -0.0562 0.0142  464 HOH   A O   
6801 O  O   . HOH   F .   ? 0.7161 0.7409 0.4769 0.0141  -0.0914 -0.0323 465 HOH   A O   
6802 O  O   . HOH   F .   ? 0.3490 0.5360 0.5174 -0.1678 0.1007  -0.1387 466 HOH   A O   
6803 O  O   . HOH   F .   ? 0.2521 0.2779 0.3800 -0.0567 0.0395  -0.0766 467 HOH   A O   
6804 O  O   . HOH   F .   ? 0.2518 0.4822 0.5472 0.0643  -0.0008 -0.1774 468 HOH   A O   
6805 O  O   . HOH   F .   ? 0.3910 0.5230 0.4670 0.0701  -0.0420 0.1392  469 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2578 0.1731 0.2773 0.0221  -0.0803 -0.0197 470 HOH   A O   
6807 O  O   . HOH   F .   ? 0.6629 0.3493 0.7221 0.0820  0.0414  0.2247  471 HOH   A O   
6808 O  O   . HOH   F .   ? 0.2527 0.2730 0.3610 -0.0846 0.0440  -0.0261 472 HOH   A O   
6809 O  O   . HOH   F .   ? 0.3674 0.4891 0.3952 -0.0753 -0.0248 -0.0007 473 HOH   A O   
6810 O  O   . HOH   F .   ? 0.7716 0.6567 0.6790 0.1433  0.1921  0.1892  474 HOH   A O   
6811 O  O   . HOH   F .   ? 0.4106 0.6341 0.4001 -0.0899 -0.0711 0.2294  475 HOH   A O   
6812 O  O   A HOH   F .   ? 0.3027 0.2417 0.5351 0.0763  -0.1975 -0.0674 476 HOH   A O   
6813 O  O   . HOH   F .   ? 0.5646 0.4739 0.4973 0.0149  0.1107  0.0386  477 HOH   A O   
6814 O  O   . HOH   F .   ? 0.5990 0.5573 0.4416 0.1209  -0.1124 -0.0860 478 HOH   A O   
6815 O  O   . HOH   F .   ? 0.4153 0.5137 0.3788 0.0622  -0.0581 -0.0818 479 HOH   A O   
6816 O  O   . HOH   F .   ? 0.3170 0.2589 0.4071 0.0186  0.0979  -0.0020 480 HOH   A O   
6817 O  O   . HOH   F .   ? 0.4222 0.4242 0.2786 -0.0145 -0.0004 -0.0123 481 HOH   A O   
6818 O  O   . HOH   F .   ? 0.4174 0.4940 0.3170 -0.0476 -0.0464 -0.0307 482 HOH   A O   
6819 O  O   . HOH   F .   ? 0.4997 0.2810 0.3331 -0.0602 -0.1312 0.0598  483 HOH   A O   
6820 O  O   . HOH   F .   ? 0.5795 0.6161 0.6155 -0.1615 -0.1345 -0.0560 484 HOH   A O   
6821 O  O   . HOH   F .   ? 0.4972 0.4294 0.5216 -0.2021 -0.0632 -0.0539 485 HOH   A O   
6822 O  O   . HOH   F .   ? 0.2534 0.2248 0.2582 0.0283  -0.0072 0.0104  486 HOH   A O   
6823 O  O   . HOH   F .   ? 0.7018 0.5664 0.6914 -0.0825 0.0532  -0.1041 487 HOH   A O   
6824 O  O   . HOH   F .   ? 0.5923 0.3891 0.4640 -0.0184 0.1346  -0.0256 488 HOH   A O   
6825 O  O   . HOH   F .   ? 0.5572 0.4245 0.4384 0.0185  -0.0174 -0.1121 489 HOH   A O   
6826 O  O   . HOH   F .   ? 0.7660 0.3929 0.3361 -0.0397 -0.1244 0.0322  490 HOH   A O   
6827 O  O   B HOH   F .   ? 0.4840 0.4750 0.4493 0.0504  -0.0937 0.0137  491 HOH   A O   
6828 O  O   . HOH   F .   ? 0.5899 0.6223 0.4466 -0.0669 0.1271  0.1222  492 HOH   A O   
6829 O  O   . HOH   F .   ? 0.2885 0.4700 0.3346 -0.0219 -0.0195 -0.0736 493 HOH   A O   
6830 O  O   . HOH   F .   ? 0.3270 0.3739 0.4654 0.0024  0.1460  0.0848  494 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2673 0.5393 0.3824 0.1202  0.0997  0.2492  495 HOH   A O   
6832 O  O   . HOH   F .   ? 0.5959 0.5463 0.6688 0.0853  0.2297  -0.1106 496 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2631 0.2393 0.7237 -0.0106 -0.1413 0.0316  497 HOH   A O   
6834 O  O   . HOH   F .   ? 0.6369 0.5067 0.4878 -0.0778 -0.1148 -0.0788 498 HOH   A O   
6835 O  O   . HOH   F .   ? 0.5249 0.5369 0.5714 0.0719  -0.0983 0.0936  499 HOH   A O   
6836 O  O   . HOH   F .   ? 0.4243 0.3532 0.4693 -0.0826 -0.0020 0.1310  500 HOH   A O   
6837 O  O   . HOH   F .   ? 0.4979 0.4059 0.2668 -0.0965 0.1660  -0.0616 501 HOH   A O   
6838 O  O   . HOH   F .   ? 0.5048 0.3170 0.5011 -0.0001 0.2512  0.0435  502 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2554 0.3376 0.5064 -0.0216 0.1007  -0.0714 503 HOH   A O   
6840 O  O   . HOH   F .   ? 0.2819 0.2194 0.6204 0.0202  0.0394  0.1063  504 HOH   A O   
6841 O  O   . HOH   F .   ? 0.6920 0.2411 0.3890 -0.0783 0.0659  0.0412  505 HOH   A O   
6842 O  O   . HOH   F .   ? 0.3698 0.7521 0.5688 -0.0868 -0.0428 0.2133  506 HOH   A O   
6843 O  O   . HOH   F .   ? 0.7077 0.6162 0.4629 0.2148  -0.1406 -0.0292 507 HOH   A O   
6844 O  O   B HOH   F .   ? 0.2101 0.3028 0.2565 0.0188  0.0621  0.0255  508 HOH   A O   
6845 O  O   . HOH   F .   ? 0.2885 0.4284 0.3366 0.1170  -0.0518 0.0510  509 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2981 0.4397 0.4832 0.0896  -0.0497 0.0196  510 HOH   A O   
6847 O  O   B HOH   F .   ? 0.3427 0.4278 0.3527 0.1043  0.0631  0.1255  511 HOH   A O   
6848 O  O   . HOH   F .   ? 0.7366 0.4063 0.5513 0.0960  -0.0005 0.1544  512 HOH   A O   
6849 O  O   B HOH   F .   ? 0.3962 0.2551 0.3612 -0.0530 0.1510  0.0381  513 HOH   A O   
6850 O  O   . HOH   F .   ? 0.5723 0.7327 0.5436 0.1411  -0.0706 0.0670  514 HOH   A O   
6851 O  O   B HOH   F .   ? 0.2319 0.3753 0.3258 0.0226  0.0288  0.0970  515 HOH   A O   
6852 O  O   . HOH   F .   ? 0.2963 0.2313 0.4835 0.0142  0.0273  0.0584  516 HOH   A O   
6853 O  O   . HOH   F .   ? 0.5475 0.6778 0.4801 0.3195  0.0144  0.1398  517 HOH   A O   
6854 O  O   T HOH   F .   ? 0.1109 0.1006 0.2504 -0.0170 -0.0266 0.0598  518 HOH   A O   
6855 O  O   A HOH   F .   ? 0.4716 0.8764 0.4158 0.2025  -0.0052 -0.0304 519 HOH   A O   
6856 O  O   . HOH   F .   ? 0.5445 0.6738 0.4750 -0.0713 -0.0434 -0.1055 520 HOH   A O   
6857 O  O   . HOH   F .   ? 0.2580 0.7555 0.4289 0.0646  0.0247  -0.0688 521 HOH   A O   
6858 O  O   B HOH   F .   ? 0.3884 0.3989 0.3436 0.1215  0.0848  0.0800  522 HOH   A O   
6859 O  O   . HOH   F .   ? 0.5329 0.4781 0.5308 0.1549  -0.0117 0.1492  523 HOH   A O   
6860 O  O   . HOH   F .   ? 0.4495 0.7149 0.5672 -0.0696 -0.0523 0.0586  524 HOH   A O   
6861 O  O   . HOH   F .   ? 0.2689 0.4611 0.5983 -0.0258 -0.0967 0.2790  525 HOH   A O   
6862 O  O   . HOH   G .   ? 0.2271 0.2230 0.3343 0.0163  0.0716  0.0339  201 HOH   B O   
6863 O  O   . HOH   G .   ? 0.4926 0.3710 0.4003 -0.0261 0.0170  -0.1449 202 HOH   B O   
6864 O  O   . HOH   G .   ? 0.3719 0.3668 0.6671 -0.0709 0.0354  -0.0011 203 HOH   B O   
6865 O  O   . HOH   G .   ? 0.2899 0.7090 0.3931 0.0718  0.0199  0.2338  204 HOH   B O   
6866 O  O   . HOH   G .   ? 0.3217 0.5555 0.5350 -0.0078 0.1890  -0.1705 205 HOH   B O   
6867 O  O   . HOH   G .   ? 0.7305 0.3257 0.4433 0.0979  0.1154  0.0258  206 HOH   B O   
6868 O  O   . HOH   G .   ? 0.4688 0.5062 0.2891 -0.0146 -0.0488 -0.1365 207 HOH   B O   
6869 O  O   . HOH   G .   ? 0.6943 0.6291 0.5916 0.2449  -0.0025 -0.0066 208 HOH   B O   
6870 O  O   . HOH   G .   ? 0.3173 0.2376 0.5251 0.0101  0.1859  0.0435  209 HOH   B O   
6871 O  O   . HOH   G .   ? 0.4782 0.6360 0.4071 0.3096  -0.0873 -0.0298 210 HOH   B O   
6872 O  O   . HOH   G .   ? 0.4756 0.3981 0.5825 0.0333  -0.0902 0.2573  211 HOH   B O   
6873 O  O   . HOH   G .   ? 0.1930 0.2281 0.3221 -0.0042 0.0266  -0.0347 212 HOH   B O   
6874 O  O   . HOH   G .   ? 0.3825 0.4260 0.5435 -0.1010 -0.0056 -0.1205 213 HOH   B O   
6875 O  O   . HOH   G .   ? 0.1654 0.1917 0.3138 -0.0157 -0.0045 0.0073  214 HOH   B O   
6876 O  O   . HOH   G .   ? 0.3770 0.3694 0.4974 0.0860  -0.0188 0.0055  215 HOH   B O   
6877 O  O   . HOH   G .   ? 0.2964 0.2813 0.6573 0.0575  -0.1115 0.0697  216 HOH   B O   
6878 O  O   . HOH   G .   ? 0.4470 0.5703 0.4380 0.2864  -0.0305 0.0163  217 HOH   B O   
6879 O  O   . HOH   G .   ? 0.5314 0.3829 0.3629 0.0012  -0.1241 0.0621  218 HOH   B O   
6880 O  O   . HOH   G .   ? 0.3326 0.5340 0.5187 0.2091  0.0375  -0.0378 219 HOH   B O   
6881 O  O   . HOH   G .   ? 0.2996 0.1998 0.5952 0.0166  0.1902  0.0782  220 HOH   B O   
6882 O  O   . HOH   G .   ? 0.4124 0.6720 0.3943 0.1476  0.0411  -0.0450 221 HOH   B O   
6883 O  O   . HOH   G .   ? 0.4368 0.4711 0.3818 0.0541  0.0726  -0.1503 222 HOH   B O   
6884 O  O   . HOH   G .   ? 0.4321 0.4489 0.6363 0.0411  -0.1542 -0.0805 223 HOH   B O   
6885 O  O   . HOH   G .   ? 0.5839 0.2910 0.4491 -0.1754 0.0159  0.0256  224 HOH   B O   
6886 O  O   . HOH   G .   ? 0.7396 0.4310 0.2757 -0.0625 0.1154  0.0096  225 HOH   B O   
6887 O  O   . HOH   G .   ? 0.4966 0.2073 0.3067 0.0164  -0.0877 -0.0022 226 HOH   B O   
6888 O  O   . HOH   G .   ? 0.2598 0.1859 0.2829 -0.0318 0.1051  -0.0027 227 HOH   B O   
6889 O  O   . HOH   G .   ? 0.2171 0.2268 0.4488 -0.0330 -0.0001 -0.0711 228 HOH   B O   
6890 O  O   . HOH   G .   ? 0.3203 0.4114 0.6156 -0.0483 0.0555  -0.0506 229 HOH   B O   
6891 O  O   . HOH   G .   ? 0.3605 0.1777 0.2289 0.0176  -0.0842 -0.0062 230 HOH   B O   
6892 O  O   . HOH   G .   ? 0.1729 0.2054 0.3326 -0.0173 0.0124  -0.0126 231 HOH   B O   
6893 O  O   . HOH   G .   ? 0.3479 0.2745 0.4334 0.0460  -0.0790 -0.1362 232 HOH   B O   
6894 O  O   . HOH   G .   ? 0.7350 0.4813 0.4816 0.2487  -0.0518 -0.1339 233 HOH   B O   
6895 O  O   . HOH   G .   ? 0.2786 0.2567 0.3291 0.0334  0.0208  -0.0825 234 HOH   B O   
6896 O  O   . HOH   G .   ? 0.5672 0.3104 0.3900 -0.2283 -0.0184 0.0211  235 HOH   B O   
6897 O  O   . HOH   G .   ? 0.2076 0.2444 0.3360 -0.0476 0.0042  -0.0221 236 HOH   B O   
6898 O  O   . HOH   G .   ? 0.3770 0.2975 0.4176 0.0958  -0.0374 -0.0728 237 HOH   B O   
6899 O  O   . HOH   G .   ? 0.7152 0.6153 0.3518 0.1173  0.0358  0.0329  238 HOH   B O   
6900 O  O   . HOH   G .   ? 0.3863 0.4404 0.5211 -0.1675 -0.0166 0.0826  239 HOH   B O   
6901 O  O   . HOH   G .   ? 0.3665 0.3125 0.2246 0.0340  0.0604  0.0406  240 HOH   B O   
6902 O  O   . HOH   G .   ? 0.2079 0.1364 0.3279 0.0065  -0.0530 -0.0036 241 HOH   B O   
6903 O  O   . HOH   G .   ? 0.2071 0.3999 0.2589 -0.0507 -0.0204 0.0617  242 HOH   B O   
6904 O  O   . HOH   G .   ? 0.2633 0.3795 0.3607 -0.0699 0.0294  -0.0458 243 HOH   B O   
6905 O  O   . HOH   G .   ? 0.1627 0.1450 0.2920 -0.0023 0.0051  -0.0062 244 HOH   B O   
6906 O  O   . HOH   G .   ? 0.1487 0.1490 0.1677 -0.0118 -0.0052 -0.0012 245 HOH   B O   
6907 O  O   . HOH   G .   ? 0.2237 0.1941 0.2230 -0.0379 -0.0477 0.0255  246 HOH   B O   
6908 O  O   . HOH   G .   ? 0.1490 0.1353 0.1832 -0.0010 -0.0071 0.0109  247 HOH   B O   
6909 O  O   . HOH   G .   ? 0.3043 0.4656 0.3071 -0.1182 -0.0233 -0.0501 248 HOH   B O   
6910 O  O   . HOH   G .   ? 0.2088 0.3900 0.3346 -0.0424 -0.0595 -0.0415 249 HOH   B O   
6911 O  O   . HOH   G .   ? 0.3197 0.1802 0.6501 -0.0160 -0.1239 -0.0279 250 HOH   B O   
6912 O  O   . HOH   G .   ? 0.3324 0.3823 0.2412 0.0314  0.0727  0.0215  251 HOH   B O   
6913 O  O   . HOH   G .   ? 0.2411 0.2199 0.2728 0.0793  -0.0837 -0.0663 252 HOH   B O   
6914 O  O   . HOH   G .   ? 0.2836 0.2110 0.3157 0.0683  0.0834  -0.0057 253 HOH   B O   
6915 O  O   . HOH   G .   ? 0.2139 0.1547 0.2251 -0.0355 -0.0388 0.0290  254 HOH   B O   
6916 O  O   . HOH   G .   ? 0.4779 0.3611 0.3782 -0.1119 0.0792  -0.1273 255 HOH   B O   
6917 O  O   . HOH   G .   ? 0.2381 0.3096 0.2246 -0.0621 0.0267  0.0251  256 HOH   B O   
6918 O  O   . HOH   G .   ? 0.2677 0.2207 0.2103 0.0112  -0.0139 0.0017  257 HOH   B O   
6919 O  O   . HOH   G .   ? 0.2433 0.1849 0.3828 -0.0017 -0.0656 -0.0379 258 HOH   B O   
6920 O  O   . HOH   G .   ? 0.2681 0.5240 0.5711 0.0051  0.0269  -0.1127 259 HOH   B O   
6921 O  O   . HOH   G .   ? 0.1609 0.1684 0.3403 -0.0280 -0.0228 0.0210  260 HOH   B O   
6922 O  O   . HOH   G .   ? 0.4240 0.2695 0.4694 -0.0199 -0.1291 -0.0556 261 HOH   B O   
6923 O  O   . HOH   G .   ? 0.3233 0.2743 0.3314 -0.0390 0.0244  -0.0527 262 HOH   B O   
6924 O  O   . HOH   G .   ? 0.4714 0.4113 0.3001 0.0006  -0.0140 -0.0872 263 HOH   B O   
6925 O  O   . HOH   G .   ? 0.2543 0.5280 0.5799 0.1574  -0.0547 -0.1038 264 HOH   B O   
6926 O  O   . HOH   G .   ? 0.1416 0.1644 0.2258 -0.0074 0.0132  0.0187  265 HOH   B O   
6927 O  O   . HOH   G .   ? 0.2528 0.3977 0.4106 0.0400  0.1199  0.0362  266 HOH   B O   
6928 O  O   . HOH   G .   ? 0.2410 0.2118 0.2166 0.0074  -0.0009 -0.0006 267 HOH   B O   
6929 O  O   . HOH   G .   ? 0.2511 0.1997 0.3058 -0.0703 0.0176  -0.0118 268 HOH   B O   
6930 O  O   . HOH   G .   ? 0.1887 0.1938 0.1829 -0.0502 -0.0434 0.0130  269 HOH   B O   
6931 O  O   . HOH   G .   ? 0.2487 0.2756 0.2737 -0.0380 -0.0805 0.0237  270 HOH   B O   
6932 O  O   . HOH   G .   ? 0.2886 0.2132 0.5377 0.0115  0.0605  0.0576  271 HOH   B O   
6933 O  O   . HOH   G .   ? 0.3306 0.5323 0.3337 -0.0424 -0.1002 0.0980  272 HOH   B O   
6934 O  O   . HOH   G .   ? 0.2189 0.4224 0.5321 -0.0539 -0.0277 -0.1530 273 HOH   B O   
6935 O  O   . HOH   G .   ? 0.1805 0.1419 0.4078 -0.0072 -0.0215 -0.0240 274 HOH   B O   
6936 O  O   . HOH   G .   ? 0.2095 0.1600 0.2345 -0.0261 -0.0138 0.0185  275 HOH   B O   
6937 O  O   . HOH   G .   ? 0.2653 0.4683 0.2284 0.1705  -0.0321 -0.0478 276 HOH   B O   
6938 O  O   . HOH   G .   ? 0.3687 0.3811 0.4874 0.1487  -0.0824 -0.1145 277 HOH   B O   
6939 O  O   . HOH   G .   ? 0.2372 0.2564 0.2501 -0.0333 -0.0645 -0.0375 278 HOH   B O   
6940 O  O   . HOH   G .   ? 0.4103 0.3696 0.5569 0.0581  0.0381  0.0020  279 HOH   B O   
6941 O  O   . HOH   G .   ? 0.2346 0.3555 0.3539 -0.0338 0.0397  -0.1162 280 HOH   B O   
6942 O  O   . HOH   G .   ? 0.2699 0.6960 0.2645 0.0889  -0.0359 -0.0550 281 HOH   B O   
6943 O  O   . HOH   G .   ? 0.1633 0.1574 0.3692 -0.0136 0.0059  0.0007  282 HOH   B O   
6944 O  O   . HOH   G .   ? 0.2865 0.6584 0.7594 0.1152  -0.0617 -0.0928 283 HOH   B O   
6945 O  O   . HOH   G .   ? 0.2719 0.4796 0.4921 -0.0957 -0.1285 0.0715  284 HOH   B O   
6946 O  O   . HOH   G .   ? 0.1717 0.1522 0.2088 0.0009  0.0108  0.0021  285 HOH   B O   
6947 O  O   . HOH   G .   ? 0.4974 0.6937 0.2636 -0.0242 -0.1088 0.0052  286 HOH   B O   
6948 O  O   . HOH   G .   ? 0.4651 0.4340 0.4883 0.0049  -0.1581 0.0002  287 HOH   B O   
6949 O  O   . HOH   G .   ? 0.1660 0.2062 0.1776 -0.0118 -0.0183 0.0132  288 HOH   B O   
6950 O  O   . HOH   G .   ? 0.2378 0.2716 0.2911 0.0021  -0.0699 0.0147  289 HOH   B O   
6951 O  O   . HOH   G .   ? 0.3514 0.2616 0.2351 0.0056  -0.0865 -0.0017 290 HOH   B O   
6952 O  O   . HOH   G .   ? 0.3942 0.2280 0.4044 -0.1039 -0.2148 0.0973  291 HOH   B O   
6953 O  O   . HOH   G .   ? 0.5617 0.3736 0.3220 0.2517  0.1166  0.0960  292 HOH   B O   
6954 O  O   . HOH   G .   ? 0.1701 0.2148 0.3149 0.0165  -0.0040 0.0172  293 HOH   B O   
6955 O  O   . HOH   G .   ? 0.1733 0.3405 0.5239 0.0227  0.0056  -0.1452 294 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3369 0.3043 0.2964 -0.0271 0.0031  -0.1247 295 HOH   B O   
6957 O  O   . HOH   G .   ? 0.4490 0.4939 0.2582 0.0173  0.0870  0.1231  296 HOH   B O   
6958 O  O   . HOH   G .   ? 0.1810 0.1664 0.2524 0.0101  0.0048  0.0144  297 HOH   B O   
6959 O  O   . HOH   G .   ? 0.5062 0.3814 0.2513 0.1396  -0.0937 0.0377  298 HOH   B O   
6960 O  O   . HOH   G .   ? 0.3292 0.2889 0.5041 -0.0502 -0.0923 0.1330  299 HOH   B O   
6961 O  O   . HOH   G .   ? 0.3531 0.1877 0.3755 0.0719  0.1292  0.0524  300 HOH   B O   
6962 O  O   . HOH   G .   ? 0.4887 0.3044 0.2346 -0.1740 0.0650  -0.0238 301 HOH   B O   
6963 O  O   . HOH   G .   ? 0.3981 0.7298 0.3739 0.1596  -0.0606 0.1211  302 HOH   B O   
6964 O  O   . HOH   G .   ? 0.3440 0.3653 0.4072 -0.1502 0.1093  -0.0392 303 HOH   B O   
6965 O  O   . HOH   G .   ? 0.2030 0.3003 0.6441 0.0486  -0.0595 -0.1123 304 HOH   B O   
6966 O  O   . HOH   G .   ? 0.2939 0.3020 0.3870 -0.0514 0.1181  -0.0976 305 HOH   B O   
6967 O  O   . HOH   G .   ? 0.2184 0.1675 0.2756 -0.0273 -0.0334 -0.0012 306 HOH   B O   
6968 O  O   . HOH   G .   ? 0.6392 0.6528 0.5182 0.3239  -0.0273 0.0013  307 HOH   B O   
6969 O  O   . HOH   G .   ? 0.3828 0.4148 0.8076 -0.0142 -0.1109 0.1948  308 HOH   B O   
6970 O  O   . HOH   G .   ? 0.2084 0.1599 0.3885 0.0371  -0.1010 0.0014  309 HOH   B O   
6971 O  O   . HOH   G .   ? 0.2309 0.3161 0.4809 -0.0168 -0.0483 -0.0111 310 HOH   B O   
6972 O  O   . HOH   G .   ? 0.1584 0.1505 0.3416 0.0060  0.0012  -0.0013 311 HOH   B O   
6973 O  O   . HOH   G .   ? 0.1663 0.1870 0.3199 -0.0303 -0.0078 0.0137  312 HOH   B O   
6974 O  O   . HOH   G .   ? 0.2502 0.1576 0.2601 -0.0165 -0.0165 0.0315  313 HOH   B O   
6975 O  O   . HOH   G .   ? 0.4313 0.2353 0.2630 0.1542  0.1066  0.0345  314 HOH   B O   
6976 O  O   . HOH   G .   ? 0.4853 0.4409 0.2773 0.0222  -0.0536 -0.0724 315 HOH   B O   
6977 O  O   . HOH   G .   ? 0.4433 0.4251 0.5601 0.0517  0.0056  0.0199  316 HOH   B O   
6978 O  O   . HOH   G .   ? 0.2391 0.2058 0.1995 -0.0124 0.0183  0.0254  317 HOH   B O   
6979 O  O   . HOH   G .   ? 0.2079 0.5691 0.4926 -0.0570 -0.0106 -0.0007 318 HOH   B O   
6980 O  O   . HOH   G .   ? 0.1606 0.1664 0.3184 -0.0123 -0.0230 -0.0122 319 HOH   B O   
6981 O  O   . HOH   G .   ? 0.1764 0.2977 0.2642 -0.0177 -0.0212 0.0800  320 HOH   B O   
6982 O  O   . HOH   G .   ? 0.4603 0.3607 0.4774 -0.0754 0.0313  0.1307  321 HOH   B O   
6983 O  O   . HOH   G .   ? 0.4775 0.2582 0.3037 0.0262  0.0339  0.0880  322 HOH   B O   
6984 O  O   . HOH   G .   ? 0.3185 0.2223 0.2535 0.0251  -0.0216 0.0343  323 HOH   B O   
6985 O  O   . HOH   G .   ? 0.1963 0.2048 0.3034 0.0318  0.0471  0.0292  324 HOH   B O   
6986 O  O   . HOH   G .   ? 0.2082 0.2384 0.5651 -0.0447 -0.0037 0.1397  325 HOH   B O   
6987 O  O   . HOH   G .   ? 0.4403 0.3243 0.5552 0.1159  0.2094  0.1868  326 HOH   B O   
6988 O  O   . HOH   G .   ? 0.4162 0.4608 0.2307 0.1207  -0.0768 -0.0198 327 HOH   B O   
6989 O  O   . HOH   G .   ? 0.6464 0.4798 0.6672 0.1583  -0.0755 0.1887  328 HOH   B O   
6990 O  O   . HOH   G .   ? 0.2853 0.3163 0.5095 -0.0583 -0.1601 0.1316  329 HOH   B O   
6991 O  O   . HOH   G .   ? 0.6599 0.4624 0.5451 0.1232  0.1495  -0.0246 330 HOH   B O   
6992 O  O   . HOH   G .   ? 0.1728 0.2842 0.3373 0.0257  -0.0118 -0.0692 331 HOH   B O   
6993 O  O   . HOH   G .   ? 0.2616 0.1963 0.5955 -0.0069 0.0052  0.0517  332 HOH   B O   
6994 O  O   . HOH   G .   ? 0.5743 0.3850 0.3890 0.0201  0.1198  0.1499  333 HOH   B O   
6995 O  O   . HOH   G .   ? 0.8239 0.2105 0.3320 0.0125  -0.0824 0.0006  334 HOH   B O   
6996 O  O   . HOH   G .   ? 0.5608 0.5713 0.5488 -0.1080 -0.0596 0.1609  335 HOH   B O   
6997 O  O   . HOH   G .   ? 0.5725 0.3536 0.4710 0.0205  0.1088  -0.1457 336 HOH   B O   
6998 O  O   . HOH   G .   ? 0.1834 0.1465 0.2576 0.0058  -0.0240 0.0075  337 HOH   B O   
6999 O  O   . HOH   G .   ? 0.5797 0.4040 0.6522 -0.0683 -0.0740 -0.1153 338 HOH   B O   
7000 O  O   . HOH   G .   ? 0.4771 0.3199 0.3245 0.0633  -0.1172 -0.0550 339 HOH   B O   
7001 O  O   . HOH   G .   ? 0.4301 0.7428 0.4190 -0.0533 -0.0667 0.2207  340 HOH   B O   
7002 O  O   . HOH   G .   ? 0.7315 0.6221 0.3138 0.0118  -0.0670 0.0985  341 HOH   B O   
7003 O  O   . HOH   G .   ? 0.3624 0.6064 0.3915 -0.0951 -0.0625 -0.0736 342 HOH   B O   
7004 O  O   . HOH   G .   ? 0.1891 0.5817 0.6640 -0.0035 -0.0757 0.0150  343 HOH   B O   
7005 O  O   . HOH   G .   ? 0.4573 0.5224 0.3717 -0.0036 -0.1059 0.0019  344 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2155 0.1933 0.3359 -0.0092 0.0590  -0.0070 345 HOH   B O   
7007 O  O   . HOH   G .   ? 0.3003 0.1890 0.4258 0.0391  -0.1284 -0.0516 346 HOH   B O   
7008 O  O   . HOH   G .   ? 0.4186 0.5537 0.5862 0.0194  -0.0863 0.0989  347 HOH   B O   
7009 O  O   . HOH   G .   ? 0.5093 0.5519 0.4977 -0.1161 0.0355  0.1295  348 HOH   B O   
7010 O  O   . HOH   G .   ? 0.4436 0.5959 0.6866 0.0226  0.0531  -0.0427 349 HOH   B O   
7011 O  O   . HOH   G .   ? 0.2703 0.6403 0.3346 0.1847  -0.0598 -0.1445 350 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2080 0.4257 0.5306 0.0285  0.0380  0.0106  351 HOH   B O   
7013 O  O   . HOH   G .   ? 0.2775 0.2280 0.4995 -0.0244 -0.1028 -0.0418 352 HOH   B O   
7014 O  O   . HOH   G .   ? 0.3683 0.2264 0.3373 -0.0643 0.0085  -0.0767 353 HOH   B O   
7015 O  O   . HOH   G .   ? 0.3434 0.4891 0.4826 -0.1513 -0.0026 -0.0513 354 HOH   B O   
7016 O  O   . HOH   G .   ? 0.4033 0.2898 0.3509 -0.1107 0.0019  -0.0553 355 HOH   B O   
7017 O  O   . HOH   G .   ? 0.5433 0.3980 0.4187 0.0608  0.1369  -0.0652 356 HOH   B O   
7018 O  O   . HOH   G .   ? 0.4461 0.2933 0.5637 -0.0944 0.1392  0.0627  357 HOH   B O   
7019 O  O   . HOH   G .   ? 0.4690 0.5381 0.4914 0.1734  -0.1136 0.1674  358 HOH   B O   
7020 O  O   . HOH   G .   ? 0.5829 0.3334 0.5055 -0.0372 -0.1427 -0.0456 359 HOH   B O   
7021 O  O   . HOH   G .   ? 0.5021 0.3627 0.6455 0.0598  0.1209  0.1316  360 HOH   B O   
7022 O  O   . HOH   G .   ? 0.4978 0.6314 0.3269 0.2483  0.0100  0.0516  361 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2308 0.3794 0.6882 -0.0847 -0.0594 -0.0753 362 HOH   B O   
7024 O  O   . HOH   G .   ? 0.5297 0.4823 0.5504 -0.0431 0.0311  0.0294  363 HOH   B O   
7025 O  O   . HOH   G .   ? 0.6395 0.2294 0.3618 -0.0041 0.0133  0.0707  364 HOH   B O   
7026 O  O   . HOH   G .   ? 0.4777 0.2999 0.6127 -0.1390 -0.0514 0.0236  365 HOH   B O   
7027 O  O   . HOH   G .   ? 0.6007 0.4649 0.4269 0.1094  0.0418  0.0753  366 HOH   B O   
7028 O  O   . HOH   G .   ? 0.5202 0.5705 0.3706 0.1588  -0.1517 0.0544  367 HOH   B O   
7029 O  O   . HOH   G .   ? 0.5394 0.5339 0.4198 -0.0735 -0.0526 -0.1104 368 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4782 0.4346 0.5337 0.1851  -0.1256 0.0148  369 HOH   B O   
7031 O  O   . HOH   G .   ? 0.4067 0.5745 0.5097 0.2474  0.1052  0.1719  370 HOH   B O   
7032 O  O   . HOH   G .   ? 0.8412 0.7878 0.5752 0.2522  -0.1371 0.0993  371 HOH   B O   
7033 O  O   . HOH   G .   ? 0.6409 0.3566 0.2966 -0.1038 -0.1008 -0.0441 372 HOH   B O   
7034 O  O   . HOH   G .   ? 0.3757 0.2973 0.4249 0.0697  -0.1270 -0.0482 373 HOH   B O   
7035 O  O   . HOH   G .   ? 0.4634 0.4866 0.4888 -0.0612 -0.0362 0.0361  374 HOH   B O   
7036 O  O   . HOH   G .   ? 0.4480 0.7261 0.5783 0.1380  0.0652  0.2959  375 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2299 0.4357 0.4224 0.0236  -0.0695 -0.0783 376 HOH   B O   
7038 O  O   . HOH   G .   ? 0.3032 0.5707 0.2227 -0.0033 0.0193  0.0208  377 HOH   B O   
7039 O  O   . HOH   G .   ? 0.5456 0.7217 0.4208 -0.1391 -0.0184 -0.1451 378 HOH   B O   
7040 O  O   . HOH   G .   ? 0.7748 0.3659 0.5066 -0.1025 -0.0767 0.0001  379 HOH   B O   
7041 O  O   . HOH   G .   ? 0.3810 0.5085 0.5435 0.0917  0.0076  0.0085  380 HOH   B O   
7042 O  O   . HOH   G .   ? 0.5607 0.6700 0.5948 -0.0240 0.1912  0.1698  381 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3308 0.2586 0.3213 0.0152  0.0290  0.0338  382 HOH   B O   
7044 O  O   . HOH   G .   ? 0.4345 0.8107 0.5365 -0.0095 0.1933  0.0584  383 HOH   B O   
7045 O  O   . HOH   G .   ? 0.4954 0.4837 0.4571 0.0155  -0.0337 -0.0492 384 HOH   B O   
7046 O  O   . HOH   G .   ? 0.7030 0.3857 0.3902 0.0980  0.1150  -0.0294 385 HOH   B O   
7047 O  O   . HOH   G .   ? 0.4987 0.3924 0.3599 -0.0222 0.0873  -0.0351 386 HOH   B O   
7048 O  O   . HOH   G .   ? 0.7437 0.5898 0.4310 0.2247  -0.0215 -0.0142 387 HOH   B O   
7049 O  O   . HOH   G .   ? 0.2382 0.4325 0.4348 -0.0723 -0.1021 -0.0063 388 HOH   B O   
7050 O  O   . HOH   G .   ? 0.6123 0.4222 0.5259 -0.0724 0.0611  -0.0258 389 HOH   B O   
7051 O  O   . HOH   G .   ? 0.4864 0.2752 0.4374 -0.1463 -0.0098 0.0286  390 HOH   B O   
7052 O  O   . HOH   G .   ? 0.3704 0.2391 0.3500 0.0716  -0.0370 0.0205  391 HOH   B O   
7053 O  O   . HOH   G .   ? 0.5438 0.4281 0.4581 0.0442  0.0657  0.0690  392 HOH   B O   
7054 O  O   . HOH   G .   ? 0.4338 0.2226 0.5312 -0.0359 0.0703  0.0524  393 HOH   B O   
7055 O  O   . HOH   G .   ? 0.2584 0.4073 0.7069 -0.1161 -0.0683 -0.0253 394 HOH   B O   
7056 O  O   . HOH   G .   ? 0.3480 0.3821 0.3958 0.0196  0.0159  -0.0698 395 HOH   B O   
7057 O  O   . HOH   G .   ? 0.4260 0.5915 0.4059 0.1206  0.0159  -0.0753 396 HOH   B O   
7058 O  O   . HOH   G .   ? 0.4546 0.4312 0.4833 0.0462  0.1095  0.0880  397 HOH   B O   
7059 O  O   . HOH   G .   ? 0.2159 0.2834 0.6207 -0.0645 -0.0945 0.0382  398 HOH   B O   
7060 O  O   . HOH   G .   ? 0.5841 0.4186 0.3164 -0.2416 -0.0445 0.1129  399 HOH   B O   
7061 O  O   . HOH   G .   ? 0.5645 0.6409 0.6276 0.1368  -0.1349 0.1750  400 HOH   B O   
7062 O  O   . HOH   G .   ? 0.5382 0.5632 0.3764 0.1956  -0.0386 -0.0379 401 HOH   B O   
# 
